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Post by kammy on Jan 1, 2011 13:17:41 GMT -5
In a hypothetical situation, we've got to think like a 'mad scientist'... 'What can we do to screw everything up and damage the world and everything in it most effectively with the least bit of cost and win the Nobel Prize in the process?' What's inside that brine shrimp's head? That's the same 'blood cell' that Carnicom is showing us... What is THAT inside the banana that's been shipped in a cargo bin with carbon dioxide infused in it to keep the bananas from turning brown? The answer is... it's a gas that's found in the ocean and becomes a part of sea life and oxygen in the water and air and it floats into the clouds, mixes with the dust from the Sahara, throw in some chemtrails and then let it rain into our water ways. We're exposed to these invisible micelles in every breath we take and their origin is from plankton/algae! Isn't that amazing!... invisible, a part of everyday breathing and eating and ironically - that's also how disease can be spread. Anything can be inside of a carbon/oxygen micelle, I knew that without even looking. Once the chemical/carbon shell dissolves or breaks apart, whatever life is inside starts its life cycle. Or, if there's a detrimental chemical inside, it does it's damage, we're in a continuous battle just by breathing. Now, if you're a mad scientist you find a way to modify these micelles... we suspect that their shell is made from DMS, DMSP, sulphur, carbon, copper... etc., etc., all the things that they should be made of, ok, ok - toss in some buckyball technology... But, the question is, if they've been modified (inside and out?) - What is the purpose of the modification? What are they doing to us? What is inside them? What are they interfering with or emulating? How can we protect ourselves? Are the 'carbon balls' acting as a 'plasmid', a pseudoplasmid?, contain proteins that affect us or causing our proteins to misfold... affecting our DNA/RNA? If I were a mad scientist - this is how I'd do it. I use something invisible, almost impossible to prove, blame it on pollution, something free that we breathe everyday and that's a natural part of us... the ultimate stealth bioweapon.
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Post by kammy on Jan 1, 2011 14:50:51 GMT -5
en.wikipedia.org/wiki/Plasmid"They are double stranded and, in many cases, circular." upload.wikimedia.org/wikipedia/commons/thumb/c/cf/Plasmid_%28english%29.svg/300px-Plasmid_%28english%29.svg.png"Plasmids are considered transferable genetic elements, or "replicons", capable of autonomous replication within a suitable host. Plasmids can be found in all three major domains, Archea, Bacteria and Eukarya.[1] Similar to viruses, plasmids are not considered a form of "life" as it is currently defined.[6] Unlike viruses, plasmids are "naked" DNA and do not encode genes necessary to encase the genetic material for transfer to a new host, though some classes of plasmids encode the sex pilus necessary for their own transfer. Plasmid host-to-host transfer requires direct, mechanical transfer by conjugation or changes in host gene expression allowing the intentional uptake of the genetic element by transformation.[1] Microbial transformation with plasmid DNA is neither parasitic nor symbiotic in nature, since each implies the presence of an independent species living in a commensal or detrimental state with the host organism. Rather, plasmids provide a mechanism for horizontal gene transfer within a population of microbes and typically provide a selective advantage under a given environmental state. Plasmids may carry genes that provide resistance to naturally occurring antibiotics in a competitive environmental niche, or alternatively the proteins produced may act as toxins under similar circumstances. Plasmids also can provide bacteria with an ability to fix elemental nitrogen or to degrade recalcitrant organic compounds which provide an advantage under conditions of nutrient deprivation. Gene therapy The success of some strategies of gene therapy depends on the efficient insertion of therapeutic genes at the appropriate chromosomal target sites within the human genome, without causing cell injury, oncogenic mutations (cancer) or an immune response. Plasmid vectors are one of many approaches that could be used for this purpose. Zinc finger nucleases (ZFNs) offer a way to cause a site-specific double strand break to the DNA genome and cause homologous recombination. This makes targeted gene correction a possibility in human cells. Plasmids encoding ZFN could be used to deliver a therapeutic gene to a pre-selected chromosomal site with a frequency higher than that of random integration. Although the practicality of this approach to gene therapy has yet to be proven, some aspects of it could be less problematic than the alternative viral-based delivery of therapeutic genes. Types They can 'parasitize' a conjugative plasmid, transferring at high frequency only in its presence. Plasmids are now being used to manipulate DNA and may possibly be a tool for curing many diseases. It is possible for plasmids of different types to coexist in a single cell. Several different plasmids have been found in E. coli. Some plasmids or microbial hosts include an addiction system or "postsegregational killing system (PSK)", such as the hok/sok (host killing/suppressor of killing) system of plasmid R1 in Escherichia coli.[8] This variant produces both a long-lived poison and a short-lived antidote. Several types of plasmid addiction systems (toxin/ antitoxin, metabolism-based, ORT systems) were described in the literature[9] and used in biotechnical (fermentation) or biomedical (vaccine therapy) applications. en.wikipedia.org/wiki/Transposon"Mariner-like elements are another prominent class of transposons found in multiple species including humans. The Mariner transposon was first discovered by Jacobson and Hartl in Drosophila[7]. This Class II transposable element is known for its uncanny ability to be transmitted horizontally in many species[8][9]. There are an estimated 14 thousand copies of Mariner in the human genome comprising 2.6 million base pairs[10]. These characteristics of the Mariner transposon have inspired the science fiction novel titled, "The Mariner Project"." **Looking up 'mariner-like elements' - is so ambiguous as to even know what that means... they're in flies and rice... probably everything? Plasmid Micelle www.informaworld.com/ampp/image?path=/716100757/747932032/tjen_a_141179_o_f0002g.pngMEND Nano-device Block copolymer micelles
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Post by kammy on Jan 1, 2011 15:32:38 GMT -5
The search criteria is - 'dissolve PEG shells': "1H NMR in CDCl3 and D2O as shown in figure 1. Since both of the PLA and PEG blocks are easily dissolved in CDCl3, the core–shell structure was not expected" CDCl3? Deuterated chloroform en.wikipedia.org/wiki/Deuterated_chloroform"Deuterated chloroform (CDCl3), is an isotopologue of chloroform (CHCl3) in which the hydrogen atom ("H") is replaced with a deuterium (heavy hydrogen) isotope ("D"). Deuterated chloroform is the most common solvent used in NMR spectroscopy." en.wikipedia.org/wiki/Chloroform"Chloroform is the organic compound with formula CHCl3. The colorless, sweet-smelling, dense liquid is a trihalomethane, and is considered somewhat hazardous. Several million tons are produced annually as a precursor to Teflon and refrigerants, but its use for refrigerants is being phased out. Marine In particular, chloroform is produced by brown seaweeds (Laminaria digitata, Laminaria saccharina, Fucus serratus, Pelvetia canaliculata, Ascophyllum nodosum), red seaweeds (Gigartina stellata, Corallina officinalis, Polysiphonia lanosa), and green seaweeds (Ulva lactuca, Enteromorpha sp., Cladophora albida).[3] Similarly, the macroalga Eucheuma denticulatum, which is cultivated and harvested on a large scale for carrageenan production, produces CHCl3,[4] as do Hypnea spinella, Falkenbergia hillebrandii, and Gracilara cornea along with seven indigenous macroalgae inhabiting a rock pool.[5] These studies show increased CHCl3 production with increased light intensity, presumably when photosynthesis is at a maximum. Chloroform is also produced by the brown alga Fucus vesiculosus, the green algae Cladophora glomerata, Enteromorpha ahlneriana, Enteromorpha flexuosa, and Enteromorpha intestinalis, and the diatom Pleurosira laevis.[6] Other studies observe CHCl3 in Fucus serratus, Fucus vesiculosis, Corallina officinalis, Cladophora pellucida, and Ulva lactuca,[7] and Desmarestia antarctica, Lambia antarctica, Laminaria saccharina, Neuroglossum ligulatum."
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Post by aqt on Jan 1, 2011 16:25:26 GMT -5
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Post by kammy on Jan 1, 2011 21:19:46 GMT -5
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Post by kammy on Jan 2, 2011 0:16:44 GMT -5
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Post by kammy on Jan 2, 2011 0:51:06 GMT -5
Photosynthesis?... I thought that was something plants did? "Could human skin be photosynthetic? www.physicsforums.com/showthread.php?t=189164Well, it looks like my suspicions were correct: Inside the Chernobyl reactor: fungus feeds on radiation www.wtnrradio.com/news/story.php?story=262But there's more... Apparently the fungus uses an unsuspected photosynthetic molecule: melanin. It's not green like light-loving plants, instead it's brown and eats gamma rays. What other organism deals with hard radiation and employs the melanin molecule? People?" "There is a type of Elysia spp. (Sea Slugs) that have specialised gut epithelial cells that allow them to take up the chloroplasts of the algae that they eat and maintain their function." wiki.answers.com/Q/Does_photosythesis_occur_inside_a_plant_cell"Does photosythesis occur in human cells? No, it does not. Human cells do not have any functional means of undergoing photosynthesis. More specifically, human cells do not contain plastids, which contain various pigments which absorb and use..." **Didn't I just talk about plastids? What if they gave us plastids, then what? lol Oh geez... photosynthesis.
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Post by kammy on Jan 2, 2011 1:04:27 GMT -5
Ferredoxin en.wikipedia.org/wiki/Ferredoxin"Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron-sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.[1][2] Another redox protein, isolated from spinach chloroplasts by Tagawa and Arnon in 1962, was termed "chloroplast ferredoxin".[3] The chloroplast ferredoxin is involved in both cyclic and non-cyclic photophosphorylation reactions of photosynthesis. In non-cyclic photophosphorylation, ferredoxin is the last electron acceptor and reduces the enzyme NADP+ reductase. It accepts electrons produced from sunlight-excited chlorophyll and transfers them to the enzyme ferredoxin:NADP+ oxidoreductase EC 1.18.1.2. Ferredoxins are small proteins containing iron and sulfur atoms organized as iron-sulfur clusters. These biological "capacitors" can accept or discharge electrons, the effect being change in the oxidation states (+2 or +3) of the iron atoms. This way, ferredoxin acts as electron transfer agents in biological redox reactions. Other bioinorganic electron transport systems include rubredoxins, cytochromes, blue copper proteins, and the structurally related Rieske proteins. Ferredoxins can be classified according to the nature of their iron-sulfur clusters and by sequence similarity."
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Post by kammy on Jan 2, 2011 1:10:50 GMT -5
4Fe-4S are Bacterial-type ferredoxins
"A group of Fe4S4 ferredoxins, originally found in bacteria, has been termed "bacterial-type". Bacterial-type ferredoxins may in turn be subdivided into further groups, based on their sequence properties. Most contain at least one conserved domain, including four cysteine residues that bind to a [Fe4S4] cluster.
During the evolution of bacterial-type ferredoxins, intrasequence gene duplication, transposition and fusion events occurred, resulting in the appearance of proteins with multiple iron-sulfur centers. In some bacterial ferredoxins, one of the duplicated domains has lost one or more of the four conserved Cys residues. These domains have either lost their iron-sulfur binding property or bind to a [Fe3S4] cluster instead of a [Fe4S4] cluster[9] and dicluster-type[10].
3-D structures are known for a number of monocluster and dicluster bacterial-type ferredoxins. The fold belongs to the α+β class, with 2-7 α-helices and four β-strands forming a barrel-like structure, and an extruded loop containing three "proximal" Cys ligands of the iron-sulfur cluster.
High-potential iron-sulfur proteins
High-potential iron-sulfur proteins (HiPIPs) form a unique family of Fe4S4 ferredoxins that function in anaerobic electron transport chains. Some HiPIPs have a redox potential higher than any other known iron-sulfur protein (e.g., HiPIP from Rhodopila globiformis has a redox potential of ca. 450 mV). Several HiPIPs have so far been characterized structurally, their folds belonging to the α+β class. As in other bacterial ferredoxins, the [Fe4S4] cluster adopts a cubane-like conformation and is ligated to the protein via four Cys residues.
Human proteins from ferredoxin family
2Fe-2S: AOX1; FDX1; FDX1L; NDUFS1; SDHB; XDH; 4Fe-4S: ABCE1; DPYD; NDUFS8;"
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Post by skyship on Jan 2, 2011 1:17:46 GMT -5
Kammy,
.......
from your earlier link:
...http://en.wikipedia.org/wiki/Teleological
"A teleology is any philosophical account which holds that final causes exist in nature, meaning that design and purpose analogous to that found in human actions are inherent also in the rest of nature. The word comes from the Greek τέλος - telos, root: τελε-, "end, purpose."...............
root telos, end purpose. telomere.....................capping or not capping the 3'Strand.
If cap, senescence sets it, if elongate with Okasaki fragments, cells live longer, immortal.
=============== and
....from you post. "http://wiki.answers.com/Q/Does_photosythesis_occur_inside_a_plant_cell
"Does photosythesis occur in human cells? No, it does not. Human cells do not have any functional means of undergoing photosynthesis. More specifically, human cells do not contain plastids, which contain various pigments which absorb and use..."
**Didn't I just talk about plastids? What if they gave us plastids, then what? lol
Oh geez... photosynthesis. "
What if we now have chloroplasts, that would provide for the photosynthesis?
From the transposons that are in the gmo foods, from the agrobacterium? those do have chloroplasts in them.
skyship
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Post by skyship on Jan 2, 2011 1:24:00 GMT -5
This is funny! and yet so true, Kammy. love that statement.....
....."You think I'm getting off subject? In a hypothetical situation, we've got to think like a 'mad scientist'... 'What can we do to screw everything up and damage the world and everything in it most effectively with the least bit of cost and win the Nobel Prize in the process?'...............
and you end the post, with this:
....."If I were a mad scientist - this is how I'd do it. I use something invisible, almost impossible to prove, blame it on pollution, something free that we breathe everyday and that's a natural part of us... the ultimate stealth bioweapon. "
Well said.
skyship
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Post by skyship on Jan 2, 2011 1:44:09 GMT -5
Reply # 285..... MEND.............. the nano..... The STR-R8 New References of Interest: Nanotechnology www.emergentcomputation.com/nano.html=========== PELGE Nanoparticles as New Carriers for the Delivery of Plasmid DNA", Nanoparticles can be an environmental hazard. This paper discusses biodegradable monomethoxy (poly-ethelene-glycol)-poly(lactide-co-glycolide)-monomethoxy(poly-ethelene-glycol) or PELGE plasmid DNA (pDNA) containing nanoparticles. The recent non-viral vector composed of nanoparticles using poly(DL-lactide-co-glycolide) or PLGA and polylacide PLA were of interest due to their biodegradability as well as the ability to protect DNA from degradation. PELGE was found to be effective. upping the anty? newer ways to enter cells. Skyship
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Post by kammy on Jan 2, 2011 9:24:51 GMT -5
Ferredoxins from Latin ferrum: iron + redoxHaven't we seen 'redox' before, last post on page 6: en.wikipedia.org/wiki/RedoxSearch criteria is - 'iron's role in oxidation' Redox"Redox (shorthand for oxidation-reduction) reactions describe all chemical reactions in which atoms have their oxidation number (oxidation state) changed. This can be either a simple redox process, such as the oxidation of carbon to yield carbon dioxide (CO2) or the reduction of carbon by hydrogen to yield methane (CH4), or a complex process such as the oxidation of sugar (C6H12O6) in the human body through a series of complex electron transfer processes." Illustration of a redox reaction The term comes from the two concepts of reduction and oxidation. It can be explained in simple terms: Oxidation is the loss of electrons or an increase in oxidation state by a molecule, atom, or ion. Reduction is the gain of electrons or a decrease in oxidation state by a molecule, atom, or ion. The two parts of a redox reaction Oxidizers Substances that have the ability to oxidize other substances are said to be oxidative or oxidizing and are known as oxidizing agents, oxidants, or oxidizers. Put another way, the oxidant removes electrons from another substance, and is thus itself reduced. And, because it "accepts" electrons, it is also called an electron acceptor. Oxidants are usually chemical elements or substances with elements in high oxidation numbers or highly electronegative substances/elements that can gain one or two extra electrons by oxidizing an element or substance (O, F, Cl, Br)." A bonfire. Combustion consists of redox reactions involving free radicals. "Reducers Substances that have the ability to reduce other substances are said to be reductive or reducing and are known as reducing agents, reductants, or reducers. That is, the reductant transfers electrons to another substance, and is thus itself oxidized. Reductants in chemistry are very diverse. Electropositive elemental metals, such as lithium, sodium, magnesium, iron, zinc, aluminium, carbon, are good reducing agents. These metals donate or give away electrons readily. Hydride transfer reagents, such as NaBH4 and LiAlH4, are widely used in organic chemistry,[1][2] primarily in the reduction of carbonyl compounds to alcohols. Another method of reduction involves the use of hydrogen gas (H2) with a palladium, platinum, or nickel catalyst. These catalytic reductions are used primarily in the reduction of carbon-carbon double or triple bonds." Iron rusting in pyrite cubes Redox reactions in biology Many important biological processes involve redox reactions. Cellular respiration, for instance, is the oxidation of glucose (C6H12O6) to CO2 and the reduction of oxygen to water. The summary equation for cell respiration is: C6H12O6 + 6 O2 → 6 CO2 + 6 H2O The process of cell respiration also depends heavily on the reduction of NAD+ to NADH and the reverse reaction (the oxidation of NADH to NAD+). Photosynthesis is essentially the reverse of the redox reaction in cell respiration: 6 CO2 + 6 H2O + light energy → C6H12O6 + 6 O2 Biological energy is frequently stored and released by means of redox reactions. Photosynthesis involves the reduction of carbon dioxide into sugars and the oxidation of water into molecular oxygen. The reverse reaction, respiration, oxidizes sugars to produce carbon dioxide and water. As intermediate steps, the reduced carbon compounds are used to reduce nicotinamide adenine dinucleotide (NAD+), which then contributes to the creation of a proton gradient, which drives the synthesis of adenosine triphosphate (ATP) and is maintained by the reduction of oxygen. In animal cells, mitochondria perform similar functions. The term redox state is often used to describe the balance of NAD+/NADH and NADP+/NADPH in a biological system such as a cell or organ. The redox state is reflected in the balance of several sets of metabolites (e.g., lactate and pyruvate, beta-hydroxybutyrate and acetoacetate), whose interconversion is dependent on these ratios. Redox cycling A wide variety of aromatic compounds are enzymatically reduced to form free radicals that contain one more electron than their parent compounds. In general, the electron donor is any of a wide variety of flavoenzymes and their coenzymes. Once formed, these anion free radicals reduce molecular oxygen to superoxide, and regenerate the unchanged parent compound. The net reaction is the oxidation of the flavoenzyme's coenzymes and the reduction of molecular oxygen to form superoxide. This catalytic behavior has been described as futile cycle or redox cycling. Examples of redox cycling-inducing molecules are the herbicide paraquat and other viologens and quinones such as menadione. [3]"
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Post by kammy on Jan 2, 2011 9:31:51 GMT -5
"What if we now have chloroplasts, that would provide for the photosynthesis? From the transposons that are in the gmo foods, from the agrobacterium? those do have chloroplasts in them. skyship" Yes, I know Sky... I'm not putting anything past them! lol I'm still looking very hard at this ferredoxin - I believe it's what we're seeing. And, if it is - it suggests that some form of photosynthesis is taking place inside of our (newly acquired ) plant material. Robert Smith has had this information out for 5 years and has anyone else mentioned it? If this is true - you think they are going to tell us?
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Post by kammy on Jan 2, 2011 10:01:07 GMT -5
The sulfur part is the natural process - the DMS(P) to DMSO to MSM... that takes place in the Sulfur Cycle. We haven't looked at the sulfur cycle yet... faculty.southwest.tn.edu/rburkett/ES%20%20we34.jpgYou can see where the trees decaying comes in...? We have to have a definite inbalance of the sulfur cycle with all that's going on, you would think? And, then they are artificially adding iron to the oceans to promote plankton blooms: Iron fertilization en.wikipedia.org/wiki/Iron_fertilization"Iron fertilization is the intentional introduction of iron to the upper ocean to stimulate a phytoplankton bloom. This is intended to enhance biological productivity, which can benefit the marine food chain and remove carbon dioxide from the atmosphere. Iron is a trace element necessary for photosynthesis in all plants." Sulfur + Iron = ferrodoxin - isn't ferrodoxin a protein? "Ferredoxins are small proteins containing iron and sulfur atoms..." Geez... in the meantime take your Zinc, folks. "Martin's famous 1991 quip, "Give me a half a tanker of iron and I will give you another ice age",[5][6] drove a decade of research whose findings suggested that iron deficiency was not merely impacting ocean ecosystems, it also offered a key to mitigating climate change as well." And... somehow the most predominate algae found in the oceans and in the plankton blooms, Synechococcus and Prochlorococcus, or something very close to them, is being seen in our samples. Our 'fungus' is a marine algae. The ferrodoxin is acting like a magnet carrier.
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Post by kammy on Jan 2, 2011 11:34:34 GMT -5
en.wikipedia.org/wiki/Iron_fertilization"The experiment was carried out in waters low in silicic acid which is likely to affect the efficacy of carbon sequestration.[22] A 900 square kilometres (350 sq mi) portion of the southwest Atlantic Ocean was fertilized with iron sulfate. A large phytoplankton bloom was triggered, however this bloom did not contain diatoms because the fertilized location was already depleted in silicic acid, an essential nutrient for diatom growth.[22] In the absence of diatoms, a relatively small amount of carbon was sequestered, because other phytoplankton are vulnerable to predation by zooplankton and do not sink rapidly upon death.[22] These poor sequestration results have caused some, including members of the LOHAFEX research team, to suggest that ocean iron fertilization is not an effective carbon mitigation strategy in general, however prior ocean fertilization experiments in high silica locations have observed much higher carbon sequestration rates because of diatom growth. LOHAFEX has just confirmed that the carbon sequestration potential depends strongly upon careful choice of location." Diatomen.wikipedia.org/wiki/Diatom"Diatoms[1] are a major group of algae, and are one of the most common types of phytoplankton. Most diatoms are unicellular, although they can exist as colonies in the shape of filaments or ribbons (e.g. Fragillaria), fans (e.g. Meridion), zigzags (e.g. Tabellaria), or stellate colonies (e.g. Asterionella). Diatoms are producers within the food chain. A characteristic feature of diatom cells is that they are encased within a unique cell wall made of silica (hydrated silicon dioxide) called a frustule." ** I believe that some of our artifacts are diatoms, they are being incorporated into the DMS/iron micelle.
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Post by kammy on Jan 2, 2011 12:05:36 GMT -5
Diatoms Facts www.buzzle.com/articles/diatoms-facts.html"Diatoms are microscopic, single-celled or colonial plant-like organisms whose cell walls are composed of silicon dioxide (silica). There are numerous holes or areolae on diatom shells (or tests) which are visible under a light microscope. Diatoms are found on damp surfaces, in the oceans, in freshwater, in lakes, streams, estuaries, puddles, wet rocks and in soils, almost anywhere where there is water and light. Most Diatoms are microscopic but some species are as long as 2 millimeters. Diatoms usually do not move, but some do move via flagellation. From diatoms classification, we know that they belong to the class Bacillariophyceae and there are more than 200 genera of living diatoms. They are classified as either protists or chromists. According to the estimates there are approximately 100,000 existing diatom species. Two types of diatoms, the round centrales and long or pen-shaped pennales are well-known. The characteristic property of diatoms which makes them unique forms of algae is that they grow a silica shell that is preserved in underwater sediments after they die. The diatom shell is known as frustule which is different for each species, so you can identify them by observing through a microscope. These frustules exhibit two asymmetrical sides with a split between them. Because of this the group is known as diatoms. Diatoms are mostly yellowish or brownish and they have chlorophylls a and c and the carotenoid fucoxanthin contained in plastids. Diatoms produce food by photosynthesis. They are great suppliers of oxygen. Diatoms reproduction is a wonderful phenomenon. Diatoms undergo asexual reproduction as they reproduce by cell division. The diatom becomes smaller with each round of replication. Read more on organisms that reproduce asexually. Diatoms facts reveal that very small diatoms may follow a sexual mode of reproduction which allows for growth of a relatively large zygote. As diatoms die they drop to the bottom. Diatom shells, not being subject to decay accumulate in the ooze and finally form the material known as diatomaceous earth."
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Post by kammy on Jan 2, 2011 14:36:12 GMT -5
alkene monooxygenase reductase Alkene monooxygenase from Mycobacterium: a multicomponent enzyme mic.sgmjournals.org/cgi/reprint/137/11/2555.pdf"Introduction Ethene-utilizing mycobacteria have been studied mainly in relation to the possibility of using them to produce optically active epoxides (Habets-Crutzen et al., 1985 ; Weijers et al., 1988; Hartmans et al., 1989). Most studies have been done with whole cells and as yet little is known about the epoxidation reaction at the enzyme level. De Bont & Harder (1978) demonstrated that the initial step in ethene metabolism in Mycobacterium E20 was the oxidation of ethene to epoxyethane by alkene monooxygenase (AMO). Low activities of AM0 were also detected in crude extracts of Mycobacterium E20 (de Bont et al., 1979). Oxidation of short-chain alkenes by methane monooxygenases also results in epoxide formation." **Epoxide formation may explain 'the glue'/epoxy: en.wikipedia.org/wiki/Epoxide
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Post by skyship on Jan 2, 2011 17:28:51 GMT -5
Smith said it was probable, not evidence. gi|56477959m(probable iron-sulfur 4Fe-4S ferredoxin protein [Azoarcus sp. EbN1]" hypothetical:Robert F. Smith - "gi|34102607conserved hypothetical protein [Chromobacterium violaceum ATCC 12472]" Has it been proven?Supp35 makes prions...............not CJD.............but URE3 those were put in environment.
Lindquist proved it could be done with metalloproteins................. there there is biotech, link.Susan Lindquist If this sounds farfetched, consider the following information from a 2004 article in the U.S. News and World Report: Susan Lindquist, director of Massachusetts Institute of Technology’s Whitehead Institute for Biomedical Research, has managed to do just this using a type of protein called a prion. “ She triggered a chain reaction in which the yeast prions spin themselves into long, durable fibers,” the article reports. “ Lindquist then genetically engineered these fibrous prions so they could bind to gold and silver nanoparticles. As she reported last spring, the result was prion fibers clad in precious metal—ultrafine conductive wires that could someday shuttle electrons around nano-size circuits.”Consider this information, as well, from the same article: “Last August [2003], the U.S. Army announced a $50 million Institute for Collaborative Biotechnologies, bringing together biotech and engineering skills from leading universities and companies. And early last month, President Bush signed the 21st Century Nanotechnology Research and Development Act, which authorizes $3.7 billion over five years — a hefty Read more: criticalbelievers.proboards.com/index.cgi?board=althealth&action=display&thread=5453#ixzz19v4o23PBskyship
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Post by kammy on Jan 3, 2011 13:46:31 GMT -5
Looking at iron fertilization again: en.wikipedia.org/wiki/Iron_fertilization"A large phytoplankton bloom was triggered, however this bloom did not contain diatoms because the fertilized location was already depleted in silicic acid, an essential nutrient for diatom growth.[22] In the absence of diatoms, a relatively small amount of carbon was sequestered, because other phytoplankton are vulnerable to predation by zooplankton and do not sink rapidly upon death." Silicic acid en.wikipedia.org/wiki/Silicic_acid"In the oceans, silicon exists primarily as orthosilicic acid (H4SiO4), and its biogeochemical cycle is regulated by the group of algae known as the diatoms.[3][4] These algae polymerise the silicic acid to so-called biogenic silica, used to construct their cell walls (called frustules). Continuing research of the correlation of aluminium and Alzheimer's disease has in the last few years included the use of silicic acid in beverages[5][6][7], due to its abilities to both reduce aluminium uptake in the digestive system as well as cause renal excretion of aluminium. Choline-stabilized orthosilicic acid is bioavailable nutritional supplement. It has been shown to prevent the loss of hair tensile strength[10], have positive effect on skin surface and skin mechanical properties, and on brittleness of hair and nails[11], abate brittle nail syndrome[12], partially prevent femoral bone loss in the aged ovariectomized rat model[13], increase collagen concentration in calves [14], and have potential beneficial effect on bone collagen formation in osteopenic females[15]." "Silicic acids may be formed by acidification of silicate salts (such as sodium silicate) in aqueous solution. When heated they lose water to form silica gel, an active form of silicon dioxide." This could explain our 'gel' part?
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Post by skyship on Jan 4, 2011 0:13:32 GMT -5
....Kammy, you said,
"Unfortunately, we don't have much real science to go by, it seems that all the independent researchers have been stopped?".................
We are the researchers, and you have done a marvelous dedicated job.
You have found many links, and an hypothesis of your making would be excellent.
I plan to publish one as well, we will come at this possibly in different directions, but, we may arrive as as Carnicom with an observation point.
So, the more hypothesis on our part, not speculation, but references to back them up we can reach some conclusions. Working hypothesis, subject to change, as Carnicom has done.
Thank you so much for all the info you gathered all in one place, bringing the earths chimeric changes in as well. because it not only effects us, but all on earth.
Another possibility for the gel is the Hydro gel, includes the hydrogen bonds, these effect oxygen and Reactive oxygen species as well. Ties in what you said about oxidation, and the aspect of lowered oxygen on earth itself.
I believe hydrogels can work like membranes. can stretch etc and in between cells, making bonds.
skyship
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Post by kammy on Jan 5, 2011 12:58:54 GMT -5
Well, thank you, Sky. I hope the people appreciate what we do, I sometimes wonder? And, all of you here deserve credit too... this is not an easy nor fun thing we do. This is troublesome that we have to look. --------------------- Here's the way I see it - in laymen's terms - These invisible gas 'bubbles' (carbon balls) can be either natural (made from the ocean the way they have been for millions of years), let's call this "A" - pseudonatural - modified by all of man's tinkerings - or man made, or a combination of all three. Or, man creates a chemical that will eventually modify or replace all the 'bubbles', except this creation has 12 or more different bacteria/algae/parasites that are now condensing instead of "A". A nanoscaled bubble can only hold so much of 'whatever' in the beginning. Its nucleus can only be programmed to do 1 thing (maybe 2), so that's why there's most likely a variety of them. These bubbles have a component of what scientists might call the 'God energy' that allows life to be created from basically thin air into a fiber, or into a crystal, or into a bacterial cell, or spore,... etc. What's the source of life - diatoms + ? (the electron)... the ferrodoxin is the spark plug, the electric spark to set life and the program in motion. The dna in the nucleus is excited by an electron to create a 'whatever' - this sets the dna expression program into pseudo-life. We need to look at dna expression, probably using the baculovirus or something like it to do this? As we've looked at the most interesting concept of a baculovirus, this is like a solar system inside of a galaxy. The galaxy is the total disease, the baculoviral part is the specific programming that can include the dna of many things. When you look at certain photos of Morgellons, what do you see? You see deep space and the ocean world, our spheres look like planets. Yes, they are like 'gods' creating worlds, unfortunately - they are inside of us now: tinypic.com/r/256fp4z/7What was in these 'bubbles' a million years ago, the natural part? That information should be out there somewhere? What's inside of them now?... anything that the dna has been sequenced plus what was there to begin with and anything it's come into contact with during the creation process. What is this creation process? It's the process of how plankton make the oxygen we breathe adding man's tinkerings and pollution.
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Post by kammy on Jan 7, 2011 15:56:35 GMT -5
This is happening this week in the German news and I did a brief search and I'm pretty sure that if I looked hard enough, dioxin can be tied to to the plankton. I can't help but believe that dioxin might also be in the mix and another chemical element we could be tested for?: Contaminated eggs found in UK food supply www.silobreaker.com/contaminated-eggs-found-in-uk-food-supply-5_2264270963120013352Germany Shuts Nearly 5000 Farms in Dioxin Scare as Officials Probe 'Illegal Activity' www.silobreaker.com/germany-shuts-nearly-5000-farms-in-dioxin-scare-as-officials-probe-illegal-activity-5_2264271648167297113Dioxin poisoning archive.student.bmj.com/issues/05/02/education/58.php"Facial rash gives a clue On his return to Ukraine, Mr Yushchenko claimed that "Ukraine's political cuisine" had tried to poison him.1 4 Ten days later, he started developing severe epidermal lesions on his face and on his torso.5 What are dioxins? Dioxins belong to a group of very robust and mostly toxic chemical compounds known as persistent organic pollutants. Easily propagated over large distances by the means of air, water, and migratory species, these chemicals have a strong tendency to bioaccumulate.6 Although they can result from natural processes, such as volcanic eruptions and forest fires, they are predominantly produced as unwanted byproducts--for example, in any combustive activity in the presence of chlorine, chlorine bleaching of pulp and paper, as well as manufacturing and processing of certain types of chemicals, such as some pesticides and herbicides.8 How are we exposed to dioxins? Dioxins are found almost everywhere.8 Once they reach the environment, they are highly persistent.7 Due to their high lipophilicity, dioxins accumulate in the adipose tissue of animals and are slowly metabolised. In humans, TCDD has an estimated half life of seven years.9 The higher you climb up the food chain, the higher the dioxin concentration you can expect to find in a given species.8 For example, when dioxin settles on water, it will rapidly accumulate in fish, rather than in other animals or plants; the same principle applies for other ecosystems. The US Environmental Protection Agency suggests that over 95% of the dioxin intake for an average human (background exposure) occurs through the ingestion of food, essentially of animal fats.7 People with vegan diets (who avoid the consumption of meat, fish, eggs, and dairy products) have significantly lower blood dioxin concentrations compared with the general population.10 Other means of exposure to dioxins include ingestion of other contaminated food, ingestion of contaminated water and soil, inhalation, and absorption through the skin.7 The most commonly affected areas of the human skin are below and to the outer side of the eye and behind the ear, although the cheeks, forehead, and neck are quite often blighted as well. The basic lesions, involving almost every hair follicle, are small infundibular cysts containing keratotic material. Hyperpigmentation often accompanies the lesions.14 Chloracne usually disappears on its own once the blood concentration of dioxin is reduced.13 Is it possible to treat dioxin poisoning? There is no regimen for TCDD detoxification. Increased faecal excretion, which already accounts for up to 50% of overall elimination of TCDD, may accelerate detoxification.17 This may be achieved with olestra, a dietary fat substitute that is neither digested nor absorbed by the human gastrointestinal tract.18 Other medicines, such as colestimide, a cholesterol lowering drug, have also been shown to decrease the blood dioxin level in humans.19 Further treatment options include symptomatic treatment, for example with isotretinoin, which may help to relieve symptoms of chloracne.20"
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Post by skyship on Jan 7, 2011 16:17:03 GMT -5
The most commonly affected areas of the human skin are below and to the outer side of the eye and behind the ear, although the cheeks, forehead, and neck are quite often blighted as well. The basic lesions, involving almost every hair follicle, are small infundibular cysts containing keratotic material.
very telling isn't it Kammy?
that keratotic material? Infundibular cysts containing kerotic material. Sounds like some our symtions?
Karretosis Follicularis or Dariers-White disease is a non-mechanical, autosomal dominant disease of late childhood. The lesions can appear a multiple papules on the heels that are cobblestone-like in appearance. Sometimes the lesions can manifest itself on the skin behind the ears. Pinpoint papules occur in relation to and in between corresponding hair follicles.
....."Hyperpigmentation often accompanies the lesions"...................
Some things might work, alcohol under the lesion or around it, would be painful, I would think, but, might work.
cytokeratin?
wonder if dimers form these? will check that out.
Thank you Kammy.
skyship
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Post by lilsissy on Jan 7, 2011 20:19:31 GMT -5
This has been coming up in my rounds lately too, monooxygenase. Involved with the opsins. Also DMSO comes up a lot too. I believe they are trying to convert us into beings that can live off the sun and also this sytem would allow for us to be read and programmed photonically. Our computers are shifting over to photonics too. en.wikipedia.org/wiki/RetinalRetinal, also called retinaldehyde or vitamin A aldehyde, is one of the many forms of vitamin A (the number of which varies from species to species). Retinal is a polyene chromophore, and bound to proteins called opsins, is the chemical basis of animal vision. Bound to proteins called type 1 rhodopsins, retinal allows certain microorganisms to convert light into metabolic energy. Vertebrate animals ingest retinal directly from meat, or produce retinal from one of four carotenoids (beta-carotene, alpha-carotene, gamma-carotene, and beta-cryptoxanthin), which they must obtain from plants or other photosynthetic organisms (no other carotenoids can be converted by animals to retinal, and some carnivores cannot convert any carotenoids at all). The other main forms of vitamin A, retinol, and a partially active form retinoic acid, may both be produced from retinal. Invertebrates such as insects and squid use hydroxylated forms of retinal in their visual systems, which derive from conversion from other xanthophylls. Living organisms produce retinal (RAL) by irreversible oxidative cleavage of carotenoids.[2] For example beta-carotene + O2 ¨ 2 retinal catalyzed by a beta-carotene 15,15'-monooxygenase[3] or a beta-carotene 15,15'-dioxygenase.[4] Just as carotenoids are the precursors of retinal, retinal is the precursor of the other forms of vitamin A. Retinal is interconvertible with retinol (ROL), the transport and storage form of vitamin A retinal + NADPH + H+ retinol + NADP+ retinol + NAD+ retinal + NADH + H+ catalyzed by retinol dehydrogenases (RDHs)[5] and alcohol dehydrogenases (ADHs).[6] Retinol is called vitamin A alcohol, or more often, simply vitamin A. Retinal can also be oxidized to retinoic acid (RA) retinal + NAD+ + H2O ¨ retinoic acid + NADH + H+ (catalyzed by RALDH) retinal + O2 + H2O ¨ retinoic acid + H2O2 (catalyzed by retinal oxidase) catalyzed by retinal dehydrogenases[7] also known as retinaldehyde dehydrogenases (RALDHs)[6] as well as retinal oxidases.[8] Retinoic acid, sometimes called vitamin A acid, is an important signaling molecule and hormone in vertebrate animals. [edit] Vision Retinal in chromophoreVision begins with the photoisomerization of retinal. When the 11-cis-retinal chromophore absorbs a photon it isomerizes from the 11-cis state to the all-trans state. The absorbance spectrum of the chromophore depends on its interactions with the opsin protein to which it is bound; different opsins produce different absorbance spectra.
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Post by lilsissy on Jan 7, 2011 20:35:05 GMT -5
wow thank you kammy for getting me to search that out here, for us!!! discovery.ucl.ac.uk/65338/Characterization of a novel human opsin gene with wide tissue expression and identification of embedded and flanking genes on chromosome 1q43 Halford, S and Freedman, MS and Bellingham, J and Inglis, SL and Poopalasundaram, S and Soni, BG and Foster, RG and Hunt, DM (2001) Characterization of a novel human opsin gene with wide tissue expression and identification of embedded and flanking genes on chromosome 1q43. Genomics , 72 (2) , 203 - 208. Full text not available from this repository. Abstract As part of an ongoing search to identify novel mammalian photopigments that may mediate nonvisual tasks such as circadian entrainment and acute suppression of pineal melatonin levels, a number of recently cloned nonvisual opsin sequences were used to search dbEST. panopsin (OPN3) was one of the clones identified using this approach. Expression analysis detects two transcripts of approximately 2.1 and 2.5 kb, in a wide range of tissues including brain, liver, and retina, which encode a predicted protein of 403 amino acids. The gene was localized to the region of chromosome 1q43 also encompassing the kynurenine monooxygenase (KMO) and choroideremia-like Rab escort protein 2 (CHML) genes. KMO and panopsin overlap at their 3' ends but are transcribed in opposite directions. CHML, an intronless gene, lies in intron 1 of panopsin end cut, that is the one I was looking for and forgot! Jen
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Post by lilsissy on Jan 7, 2011 20:50:08 GMT -5
looking up OP3 and RAB2 with GPTase anthrax gave an interesting result novel gene from alternate splicing www.ncbi.nlm.nih.gov/sites/entrez?db=pubmed&cmd=search&term=8336731&dopt=band monooxygenase brings to mind a long standing question I have , If we have agrobacteria infections as has been shown well agrobacteria fix nitrogen where they go so but this caught my eye too... Nitrifying Bacteria. Degradation of organic material typically results in the release of ammonia (NH3) into the environment. and nitrifying bacteria are more than willing to make a living oxidizing ammonia. They are ubiquitous in the environment and have even been discovered living in the sandstone of the Cologne Cathedral in Germany - The bacteria penetrate to depths of 15 cm in the sandstone blocks. These bacteria generate energy by oxidizing reduced forms of nitrogen to NO2 or NO3. The concentration of nitrifiers depends upon the rate of NH3 production in the surrounding environment. The faster the rate, the higher the population of microbes. We will briefly look at the biochemistry of two nitrifiers, Nitrosomonas and Nitrobacter Nitrosomonas oxidizes ammonia in the following reaction... NH3 + 1 1/2 O2 HNO2 + H2O Figure 1 - The reduction of ammonia by nitrifying bacteria Extracted electrons are donated directly to an ETS and no carrier is involved. The result of running the ETS is that a proton gradient is formed which can then synthesize ATP using ATP synthase. Figure 2 - Energy generation in Nitrosomonas. Only two enzymes, ammonia monooxygenase (AMO) and hydroxylamine oxidoreductase (HAO) are involved in the oxidation of ammonia to nitrite. Nitrite can be further acted on by another nitrifying bacteria, Nitrobacter. This microbe oxidizes nitrite to nitrate using oxygen as the terminal electron accepter. A proton gradient is established with resultant synthesis of ATP. Nitrobacter is often found in tandem with Nitrosomonas since the end product of Nitrosomonas metabolism is the energy substrate for Nitrobacter. This type of loose association is probably common in the environment and in this case benefits both organisms. Nitrobacter is provided with substrate and Nitrosomonas has its end product removed, which helps drive its metabolism.
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Post by lilsissy on Jan 7, 2011 21:21:28 GMT -5
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Post by skyship on Jan 7, 2011 21:42:33 GMT -5
Invertebrates such as insects and squid use hydroxylated forms of retinal in their visual systems, which derive from conversion from other xanthophylls. hydroxylated forms of retinal =============== Hydroxylation reactions play a very important role in the synthesis of cholesterol from squalene and in the conversion of cholesterol into steroid hormones and bile salts. All these hydroxylations require NADPH and O2. The oxygen atom of the incorporated hydroxyl group comes from O2 rather than from H2O. While one oxygen atom of the O2 molecule goes into the substrate, the other is reduced to water. The enzymes catalyzing these reactions are called monooxygenases (or mixed-function oxygenases). Recall that a monooxygenase also participates in the hydroxylation of aromatic amino acids (Section 23.5.7). xanthophyllsImage ch26fu16.jpg Hydroxylation requires the activation of oxygen. In the synthesis of steroid hormones and bile salts, activation is accomplished by a cytochrome P450, a family of cytochromes that absorb light maximally at 450 nm when complexed in vitro with exogenous carbon monoxide. These membraneanchored proteins (~50 kd) contain a heme prosthetic group. Because the hydroxylation reactions promoted by P450 enzymes are oxidation reactions, it is at first glance surprising that they also consume the reductant NADPH. NADPH transfers its high-potential electrons to a flavoprotein, which transfers them, one at a time, to adrenodoxin, a nonheme iron protein. Adrenodoxin transfers one electron to reduce the ferric (Fe3+) form of P450 to the ferrous (Fe2+) form (Figure 26.26). Without the addition of this electron, P450 will not bind oxygen. Recall that only the ferrous form of hemoglobin binds oxygen (Section 10.2.1). The binding of O2 to the heme is followed by the acceptance of a second electron from adrenodoxin. The acceptance of this second electron leads to cleavage of the O–O bond. One of the oxygen atoms is then protonated and released as water. The remaining oxygen atom forms a highly reactive ferryl (Fe ═ O) intermediate. This intermediate abstracts a hydrogen atom from the substrate RH to form R•. This transient free radical captures the OH group from the iron atom to form ROH, the hydroxylated product, returning the iron atom to the ferric state.Figure 26.2 6. Cytochrome P450 Mechanism.Figure 26.26 Cytochrome P450 Mechanism. These enzyme-bind O2 and use one oxygen atom to hydroxylate their substrates. 26.4.3The Cytochrome P450 System Is Widespread and Performs a Protective FunctionThe cytochrome P450 system, which in mammals is located primarily in the endoplasmic reticulum of the liver and small intestine, is also important in the detoxification of foreign substances (xenobiotic compounds) by oxidative metabolism. For example, the hydroxy lation of phenobarbital, a barbiturate, increases its solubility and facilitates its excretion. Likewise, polycyclic aromatic hydrocarbons are hydroxylated by P450, providing sites for conjugation with highly polar units (e.g., glucuronate or sulfate), which markedly increase the solubility of the modified aromatic molecule. www.ncbi.nlm.nih.gov/books/NBK22339/#A3661=================== so along with the polycyclic hydrocarbon *PAHs a flavoproteinThese aromatic, or flavoprotein are artificial. And are conjugated to the p450 chromosome. ================= I do wonder of the PAHs the kerogen form has been used in the buckyball formations. That would mean the carbon connection would as shown above by Kammy and Lil sis, to be as Smith has hypothesized. And Carnicom found, in looking at the comparisons above one can see the core, but inside the core would be the altering devices of sorts.I s it a euchromoatin or a heterchromatin?It appears it is in histone 3 where the urchin H3.3 was used and the one hypoth by Smith was another. Could both have been used? and histone 4 was altered as well.================ Why the revisit? found something? I bet they did!=================== Heterochromatin revisitedShiv I. S. Grewal and Songtao Jia Abstract | The formation of heterochromatin, which requires methylation of histone H3 at lysine 9 and the subsequent recruitment of chromodomain proteins such as heterochromatin protein HP1, serves as a model for the role of histone modifications and chromatin assembly in epigenetic control of the genome. Recent studies in Schizosaccharomyces pombe indicate that heterochromatin serves as a dynamic platform to recruit and spread a myriad of regulatory proteins across extended domains to control various chromosomal processes, including transcription, chromosome segregation and long-range chromatin interactions.========= Although epigenetic gene silencing has become almost synonymous with heterochromatization, there are several reports in the literature in which hetero- chromatin formation is required for activation of gene expression. Histone H3 methylated at lysine 9 (H3K9me) and the heterochromatin protein HP1, which are necessary for the formation of heterochromatin, have been found in association with a subset of transcribed genes. Furthermore, it has been shown that het- erochromatin proteins recruit factors that facilitate the access of RNA polymerase II (Pol II) to heterochromatic loci24 . In view of the multifaceted role of heterochroma- tin in diverse cellular functions that in some instances involve opposing cellular activities24 , our accepted concepts about heterochromatin need to be redefined.WHAT is that subset of Transcribe genes related to histone 3 and the heterchromatin? . ...."Histone H3 methylated at lysine 9 (H3K9me) and the heterochromatin protein HP1, which are necessary for the formation of heterochromatin, have been found in association with a subset of transcribed genes" So these were transcribed or read from the dna, like the mem does, mirrors the information. That subset formed from the mirror reflection of the real native, produced what type of form? ...."(H3K9me) and the heterochromatin protein HP1, "... =================== Has to do with disrupting hydrogen bonds, hydro: water, gen, generator ================== ... factor bound to histone H3 methylated on lysine 9 (H3K9me). Local changes in histone-tail modifications are not apparent. ... from chromatin by disrupting hydrogen bonds that fold its chromodomain around H3K9me. Inhibition of casein kinase 2 (CK2), an enzyme .. ============= . ...."phosphorylation of HP1-beta on amino acid Thr 51 accompanies mobilization, releasing HP1-beta from chromatin by disrupting hydrogen bonds that fold its chromodomain around H3K9me. Inhibition of casein kinase 2 (CK2), an enzyme implicated in DNA damage sensing and repair, suppresses Thr 51 phosphorylation and HP1-beta mobilization in living cells. CK2 inhibition, or a constitutively chromatin-bound HP1-beta mutant, diminishes H2AX phosphorylation. Our findings reveal an unrecognized signalling cascade that helps to initiate the DNA damage response, altering chromatin by modifying a histone-code mediator protein, HP1, but not the code itself.;'............. HP1-beta mobilization promotes chromatin changes that initiate the DNA damage response. www.epidna.com/showabstract.php?pmid=18438399=========== So HP1 beta? ? skyship this is so immense, but, between the old books and the internet we are getting closer to actually indicating that Smith's probables and hypotheticals could be the facts. However, only examining every enzyme, protein, peptide used in the Morgellons organism(s) would indicate this. Dermatopathologists have the equipment to see this, and have for a long time. Why will they not help us? Well, knowing that dark field microscopy can reveal many of the characteristics of Morgellons, including the membrane wall formed by one kind of organism
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Post by lilsissy on Jan 7, 2011 23:06:00 GMT -5
I am so glad you have a deper understanding of these things sky, I can see they are pieces but how they fit often escapes me. This is fasinating work here kammy while looking back for the split tail fungus I once found, I believe this fungus may have been mixed with something else for use on marijuana crops and it had me wondering what other bug , veg , crop... they put it in I found this, great bet it is a piece how do the opsins fits here? morgellons2.wordpress.com/For sure fungus speads out polymers.... nano polymer. The type of fungus used on the drug crops was very elusive .
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