Human Anatomy, Physiology, and Medicine. Anything human!
i have heard conflicting reports on just what exactly the fibers are comprised of... cellulose or silicon?... organic or non-organic?... can anyone elaborate?...
one of the blogs on mw says the fibers are non-organic and have high thermal properties (fire/heat resistant)... and so their argument is that they could not possibly have been produced from within the human body...
http://morgellonswatch.wordpress.com/20 ... primetime/
but look at one method used to wound and dose wheat embryos with agrobacterium... what could this imply?...
or, are the fibers comprised of cellulose and more along the lines of fungal hyphae?... look at how this species of agrobacterium causes hairy root syndrome and creates a perfect home for certain species of heterodera...
agrobacterium can mediate fungi as well as plants and crops...
http://www.ncbi.nlm.nih.gov/entrez/quer ... t=Abstract
and, some species of fungi are natural nematode killers... evidentally, the nematodes are actually attracted to the fungi...
and, meloidogyne and heterodera juveniles are also used to vector agrobacterium...
http://www.blackwell-synergy.com/links/ ... 043.x/abs/
there is a connection here somewhere people... we need to focus on it and find it...
I agree. The agrobacterium looks like the pods type things we get and. the fiber is in there also.
Now, if the fibers were our protein leaving the body, then how did it get that way? Why would it be forced to leave our nerves or muscles as protein, unless the agrobacterium has a gene altering transferon in it. If we can find the original patent on the agrobacterium, the Promoter gene, the transferon, and operon that causes the quorum sensing to take place, then maybe we can find exactly what the fiber is.
The other scenario would be that the fiber is a catalyst and is used as a transfer to us by way of non organic fiber, and the only way that could be done would be by chemtrail spraying or by being included in the shotgun DNA transfer to the plants we eat. Then it would be in our gut, from there it would move around the body, either looking for proteins to destroy, or for DNA mutation into the human being by way of gut biofilm. Now, this is done by way of replacing the protein. So, if it replaces and destroys a protein's life force, then does the protein as it dies, leave our bodies?
The other thing is the protein shotgunned into the plants could be attracting other insects and worms to live inside the plant itself. If you look at potatoes, and radishes, you can see how they have changed. The plants with stalks, broccoli, corn,
cauliflower, etc. The celery has changed, it has lost it's groove.
Does that make sense?
If not please come on back at me.
Skytroll and Maf- whoa ho ho> Good Job and thank you!
Sky, yeah let's go to the conference! Lord, I would go postal on them! haha That first one started today Sky in La Jolla!
OKAY don't miss this: It's some stuff I put together on the fibers!
Check it out:
Here is some more info I have on fibers! A must see.
http://www.verrillon.com/HARSH%20COATIN ... burn%3F%22
and oh my, check this one out:
This is similar to the one above, but it explains it better.
Next, it's textile fibers and their conversion
Dont miss this one! NASA device gives a new dimension to cell science it's the health bioreactor!! YIPPY....
or this other format:
Then this one is on silicone for water logged wood and rope
and OMG, look! it's states the "Ebola Virus and also talks about an intestinal parasite from imported fruit."Bioreactor: Ground-based research results"
okay, now this is a photo and brief synopsis of the "Tools" they play with......NOTE* make sure you scroll down to the last paragraph titled
the "commercial Sector" and click on the the hyperlink in the middle of that paragraph>man, this explains it even farther.
and what in the hell is this????????? rollercell? Hmmmmm.....
Now here you go, it's the full spectrum too><>>>>> It's the Genetic Codes!
http://www.ncbi.nlm.nih.gov/Taxonomy/Ut ... ode=c#SG11
and for what it's worth, here is something else that is kind of interesting.
http://www.biocompare.com/contents/0/Bi ... icles.html
and lastly, from the above, I got this:
The Proteomics Workhorse: Ion Trap Mass Spectrometers
Skytroll, 4 you:
http://www.bdal.com/modux3/modux3.php?p ... eight=1024
and this too:
http://www.ncbi.nlm.nih.gov/Taxonomy/Br ... e=1&unlock
National Institutes of Health
In 1994, NASA and the National Institutes of Health signed an interagency agreement to provide NASA bioreactor technology to NIH and to establish a joint Center for Three Dimensional Tissue Culture at the National Institute of Child Health and Human Development. Since the original agreement, the bioreactor has been incorporated into more than a dozen laboratories within NIH.
The bioreactor is an excellent example of how the skills and resources of two distinctly different agencies can complement each other for the public good. Where NASA is chartered to explore and exploit space, NIH is chartered to develop tools to defeat disease.
This new center is conducting 16 bioreactor research projects. Foremost among these is the first in vitro tissue system permitting the study of the HIV pathway through the human lymphatic tissue. The other 15 projects address a range of human health issues. NASA bioreactor technology is used within several NIH institutes and other agencies covering virtually all of human health: allergies, dentistry, the human genome, digestive and kidney disease, neurology, and heart, lung, and circulatory health.
At the NASA/NIH Center for Three Dimensional Tissue Culture, scientists use tonsil tissue to grow live Human Immunodeficiency Virus (HIV-1) ( how nice of them!? )and thus observe more closely the transmission of the virus. The cultures have demonstrated the same progressive loss of CD4 T-cells as seen in AIDS patients. The NASA/NIH Center also is studying an intestinal parasite found on some imported fruit.
I hope I'm helping now, what do you think Randy? See, it's not all London, London, London, it's more like Greedy Biotech and
a hateful, sneaky, lying gov't that allows this.
Last edited by London on Wed Oct 04, 2006 1:49 am, edited 1 time in total.
some useless disinformation to add to an illness on some planet in orbit around some human EGO?
Regulation of Fungal Invasive Growth
Abstract: This research project investigates the regulation of invasive growth in fungal organisms. In mammals, the ability to invade normal tissue barriers is an important attribute of metastatic cancer cells and of cells in the developing embryo. In contrast, in the adult regulatory interactions with the substratum control cell proliferation and apoptosis. This regulation by substratum is commonly lost upon malignant transformation. The goal of this research is to understand regulatory interactions with substratum. The fungi Candida albicans and Saccharomyces cerevisiae will be used as model systems because fungal cells also interact with substratum. In the opportunistic pathogen, C. albicans, interactions with the substratum may be important in promoting invasive growth of the organism within the tissues of a host. Thus, studies of C. albicans invasive growth will also contribute to the understanding of a process that plays an important role in disease. C. albicans responds to the presence of substratum by producing invasive filamentous hyphae, which penetrate into the matrix. Culture of C. albicans cells within surrounding matrix promotes rapid production of hyphae. Genetic analysis of this process has led to the identification of two gene products that are needed for normal hyphal production in response to surrounding matrix. S. cerevisiae also responds to the presence of substratum by undergoing invasive growth, although, in this organism, invasion is not associated with a dramatic change in morphology. S. cerevisiae homologues of the C. albicans genes described above are needed for normal invasive growth. Therefore, studies in S. cerevisiae will be performed in order to develop detailed molecular hypotheses for the function of the genes. Studies in C. albicans will test the generality of the hypotheses developed in S. cerevisiae. Experiments are proposed to identify interactors that bind to the gene products of interest and to elucidate the pathways in which these gene products participate.
Title: Silk Protein Polymer Designs for Improved Expression and Processing
Abstract: Silk fibers formed by insects and spiders are noted for their remarkable mechanical properties as well as their durability and biocompatibility. The exceptional solubility in vivo (20-30% w/v) of these proteins is dictated by both the need to produce solid fibers with a high packing fraction and the high mesogen concentration required for lyotropic liquid crystalline spinning, while also achieving high end mechanical properties for survival (orb webs, cocoons). A further design requirement for silk proteins is the predominance of hydrophobic amino acid residues to provide for hydrophobic interactions, water exclusion, and beta-crystallite formation to produce these strong insoluble threads. Thus the domain structure of silk proteins to accommodate high solubility of hydrophobic proteins in aqueous solution but also to permit the formation of water-insoluble final products (fibers) is critical. Additionally, silk proteins need to avoid premature precipitation as β-sheets during storage and processing. Combining knowledge of the solution state behavior, protein folding requirements and silk genetic/protein designs employing complex block-copolymer attributes, offers new experimental directions in the construction, expression and assembly of silk proteins that can help overcome longstanding limitations with silk production in heterologous systems. These studies also offer unique opportunities to marry processing environment (water) with gene designs (mimickitig silk block designs) to optimize outcomes during intracellular and extracellular processing of these complex proteins. The result of this new insight has the potential to lead to substantively improved synthesis, recovery and processing of recombinant silk proteins into Useful fibers and other silk-based materials. Our objective in the present proposal is to determine the relationships between genetic/protein block designs gleaned from our recent domain mapping studies of all silk proteins, coupled with the limitations imposed by an all aqueous processing environment based on our recent models of how silk proteins are assembled in solution toward gel states and then spinning. These issues are addressed in concert with codon optimization, expression in thermophilic hosts that can accommodate GC-rich genes and glycine/alanine overproducing mutants.
The rational design of silk encoding genes, borrowing from the more generic designs identified in Nature, in combination with the processing constraints for these proteins in Nature, highlight the novel and important design limitations and benefits offered by these intriguing protein spinning systems. The general rules of construction for silk proteins based on these observations should provide a useful guide to how Nature has solved the problem of processing hydrophobic proteins in water, and how this process can be copied industrially. The significance of the proposed studies is that by employing these design rules there should be improved expression, recovery of soluble protein and control of processing into high solids solutions and gels leading to spinnable dopes for fibers, films or other material outcomes. The insights to be gained from the proposed studies have implications in fundamental structural biology as well as direct utility toward improved options in silk-based polymer synthesis, processing and materials fabrication.
http://www.tufts.edu/central/research/R ... r05g-l.htm
Tufts University: Research News _at_ Tufts
Thanks. I had that one before but lost it, thanks a lot. Hey, check this lil puppy out......very short too:
http://www.geneservice.co.uk/products/a ... /index.jsp
http://www.geneservice.co.uk/services/s ... ervice.jsp
OKAY, I'm ticked now! Thanks for the verification.
So the next step beyong the blasted transcription is to preserve the modification. Isn't that great!
I still know how abbreviations work. ha ha...
Used to be only names for companies, now the whole DNA coding is all abbreviations, and all the little 3 letter codes of the codes.
"With ETD, scientists are enabled for specific information-rich PTM (post-translational modifications) analysis on the unsurpassed HCTultra PTM Discovery System™. ETD allows peptide and protein fragmentation while preserving modifications such as phosphorylation or glycosylation. This gives the researcher easy access to protein sequencing and simultaneous identification of type and location of various PTMs."
from your link..........
So, the phosphorylation and glycosylation, those would be the processes.
Now, just what do those two words mean?
Phosphorylation is the addition of a phosphate (PO4) group to a protein or a small molecule or "the introduction of a phosphate group into an organic molecule." Its prominent role in biochemistry is the subject of a very large body of research (as of January 2006, the Medline database returns over 120,000 articles on the subject, largely on protein phosphorylation).
In eukaryotes, protein phosphorylation is probably the most important regulatory event. Many enzymes and receptors are switched "on" or "off" by phosphorylation and dephosphorylation. Phosphorylation is catalyzed by various specific protein kinases, whereas phosphatases dephosphorylate...
.....Adding a phosphoryl (PO3) to a polar R group of an amino acid might not seem like it would do much to a protein, but it can actually turn a nonpolar hydrophobic protein into a polar and extremely hydrophilic molecule.
An example of the important role that phosphorylation plays is the p53 tumor suppressor gene, which—when active—stimulates transcription of genes that suppress the cell cycle, even to the extent that it undergoes apoptosis. However, this activity should be limited to situations where the cell is damaged or physiology is disturbed. To this end, the p53 protein is extensively regulated. In fact, p53 contains more than 18 different phosphorylation sites.
Upon the deactivating signal, the protein becomes dephosphorylated again and stops working. This is the mechanism in many forms of signal transduction, for example the way in which incoming light is processed in the light-sensitive cells of the retina.
The network underlying phosphorylation can be very complex. In some cellular signalling pathways, a protein A phosphorylates B, and B phosphorylates C, but A also phosphorylates C directly, and B can phosphorylate D, which may in turn phosphorylate A.
Protein phosphorylation sites
There are thousands of distinct phosphorylation sites in a given cell since: 1) There are thousands of different kinds of proteins in any particular cell (such as a lymphocyte). 2) It is estimated that 1/10th to 1/2 of proteins are phosphorylated (in some cellular state). 3) Phosphorylation often occurs on multiple distinct sites on a given protein.
Since phosphorylation of any site on a given protein can change the function or localization of that protein, understanding the "state" of a cell requires knowing the phosphorylation state of its proteins. For example, if amino acid Serine-473 ("S473") in the protein AKT is phosphorylated AKT is generally functionally active as a kinase. If not, it is an inactive kinase. Antibodies can be used as powerful tools to detect whether a protein is phosphorylated at any particular site. Such antibodies are called phospho-specific antibodies; 100s of such antibodies are now available. They are becoming critical reagents both for basic research and for clinical diagnosis.
Types of phosphorylation
See also protein kinase for more details on the different types of phosphorylation
Within a protein, phosphorylation can occur on several amino acids. Phosphorylation on serine is the most common, followed by threonine. Tyrosine phosphorylation is relatively rare. However, since tyrosine phosphorylated proteins are relatively easy to purify using antibodies, tyrosine phosphorylation sites are relatively well understood. Histidine and aspartate phosphorylation occurs in prokaryotes as part of two-component signalling..
ATP, the "high-energy" exchange medium in the cell, is synthesized in the mitochondrion by addition of a third phosphate group to ADP in a process referred to as oxidative phosphorylation. ATP is also synthesized by substrate-level phosphorylation during glycolysis. ATP is synthesized at the expense of solar energy by photophosphorylation in the chloroplasts of plant cells.
Phosphorylation of sugars is often the first stage of their catabolism. It allows cells to accumulate sugars because the phosphate group prevents the molecules from diffusing back across their transporter.
The Epigenome Network of Excellence (NoE)
Mammalian Phosphorylation Resource, which integrates information on available phospho-specific antibodies
Protein primary structure and posttranslational modifications
General: Protein biosynthesis | Peptide bond | Proteolysis | Racemization | N-O acyl shift
N-terminus: Acetylation | Formylation | Myristoylation | Pyroglutamate
C-terminus: Amidation | Glycosyl phosphatidylinositol (GPI)
Lysine: Methylation | Acetylation | Hydroxylation | Ubiquitination | SUMOylation | Desmosine
Cysteine: Disulfide bond | Prenylation | Palmitoylation
Serine/Threonine: Phosphorylation | Glycosylation
Tyrosine: Phosphorylation | Sulfation
Asparagine: Deamidation | Glycosylation
Aspartate: Succinimide formation
Arginine: Citrullination | Methylation
←Amino acids Secondary structure
This is about altering proteins......biosynthesis.....like biosynthesis of drugs that mimic nature. Not true natural products.
Same with our protein. I am onto this blasted protein thing, because the fiber is a protein, I bethcha.
Now along with epigenetics we have epigenomics, another word for Eugenics. Newer word, more civil, more deceitful, more cunning, more hidden they think.
I am glad the Monarchs are back in the UK.
I bet they are modified like we are. But, we love them anyway.
Now the N-terminus and the C-terminus are the target points, I think? where the modification takes place. The junctions where the evil act occurs.
Will read other.
There must be something wrong with real silk now, could it just be those cotton fiber worms are still chomping away? Or is it too dangerous now living in the the silk, because of all the BT and Wolbachia in the worms? Houston, we have a problem, so lets go synthetic and have high yield, high risks to humans. Excellent!
"The general rules of construction for silk proteins based on these observations should provide a useful guide to how Nature has solved the problem of processing hydrophobic proteins in water, and how this process can be copied industrially. The significance of the proposed studies is that by employing these design rules there should be improved expression, recovery of soluble protein and control of processing into high solids solutions and gels leading to spinnable dopes for fibers, films or other material outcomes."
Thanks for the posts, earlier, digesting them, YUCK, huh?
Will read your others.
You may have posted this before, but here it is again:
connect to rickets. Is a phophatase wasting disease.
hey befoursystemic whatch london pull a skytrol out of a disinformed hat not behind barz.....
could the wasp package morph to protamines like russian doll???not a single mode of life left gets out of the gene shuffle.................................this psycho bitches theory is leaning to
form a kingdom shift that is encoded in the wasp package per genetic combinatory stealth protocal ... like to morph from virus on an insect egg the viral plasmodia is triggered to its next form only when its host is of plant kingdom (for certain production needs) and after the gene mod complete its respired by plantkingdom to aerosol (by fungal spore) where it gains oxygen and nitrogen in clouds and morphs by condensation into its next stage into the rain, where it combines again into a complex algea with multi kingdom intellect to finish its birth and begin its life in the human at the expence of the human for the desire of the devil.
metals on sulfur with extra salt...................
A Lithium-Sensitive andSodium-Tolerant3'-Phosphoadenosine-5'-Phosphatase Encoded by halA from the Cyanobacterium Arthrospira platensis Is Closely Related to Its Counterparts from Yeasts and Plants.
"3'-Phosphoadenosine-5'-phosphatase (PAPase) is required for the removal of toxic3'-phosphoadenosine-5'-phosphate (PAP) produced during sulfur assimilation in various eukaryotic organisms. This enzyme is a well-known target of lithium and sodium toxicity and has been used for the production of salt-resistant transgenic plants. In addition, PAPase has also been proposed as a target in the treatment of manic-depressive patients. One gene, halA, which could encode a protein closely related to the PAPases of yeasts and plants, was identified from the cyanobacterium Arthrospira (Spirulina) platensis. Phylogenic analysis indicated that proteins related to PAPases from several cyanobacteria were found in different clades, suggesting multiple origins of PAPases in cyanobacteria.
The HalA polypeptide from A. platensis was overproduced in Escherichia coli and used for the characterization of its biochemical properties. HalA was dependent on Mg(2+) for its activity and could use PAP or 3'-phosphoadenosine-5'-phosphosulfate as a substrate. HalA is sensitive to Li(+) (50% inhibitory concentration [IC(50)] = 3.6 mM) but only slightly sensitive to Na(+) (IC(50) = 600 mM). The salt sensitivity of HalA was thus different from that of most of its eukaryotic counterparts, which are much more sensitive to both Li(+) and Na(+), but was comparable to the PAPase AtAHL (Hal2p-like protein) from Arabidopsis thaliana. The properties of HalA could help us to understand the structure-function relationship underlying the salt sensitivity of PAPases. The expression of halA improved the Li(+) tolerance of E. coli, suggesting that the sulfur-assimilating pathway is a likely target of salt toxicity in bacteria as well."
http://www.knockoutscience.com/showabst ... d=16391050
"Protamines and male infertility"
"Protamines are the major nuclear sperm proteins. The human sperm nucleus contains two types of protamine: pro-tamine 1 (P1) encoded by a single-copy gene and the family of protamine 2 (P2) proteins (P2, P3 and P4), all also encoded by a single gene that is transcribed and translated into a precursor protein. The protamines were discovered more than a century ago, but their function is not yet fully understood. In fact, different hypotheses have been proposed: condensation of the sperm nucleus into a compact hydrodynamic shape, protection of the genetic message delivered by the spermatozoa, involvement in the processes maintaining the integrity and repair of DNA during or after the nucleohistone-nucleoprotamine transition and involvement in the epigenetic imprinting of the spermatozoa. Protamines are also one of the most variable proteins found in nature, with data supporting a positive Darwinian selection. Changes in the expression of P1 and P2 protamines have been found to be associated with infertility in man. Mutations in the protamine genes have also been found in some infertile patients. Transgenic mice defective in the expression of protamines also present several structural defects in the sperm nucleus and have variable degrees of infertility. There is also evidence that altered levels of protamines may result in an increased susceptibility to injury in the spermatozoan DNA causing infertility or poor outcomes in assisted reproduction. The present work reviews the articles published to date on the relationship between protamines and infertility."
sticky human pig t-shirt sale........ buy 1 get 115 free
TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei.
Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.
Transgenic sterility in Populus:
expression properties of the poplar PTLF, Agrobacterium NOS and two minimal 35S promoters in vegetative tissues.Transgenic sterility is a desirable trait for containment of many kinds of transgenes and exotic species. Genetically engineered floral sterility can be imparted by expression of a cytotoxin under the control of a predominantly floral-tissue-specific promoter. However, many otherwise desirable floral promoters impart substantial non-floral expression, which can impair plant health or make it impossible to regenerate transgenic plants. We are therefore developing a floral sterility system that is capable of attenuating undesired background vegetative expression. As a first step towards this goal, we compared the vegetative expression properties of the promoter of the poplar (Populus trichocarpa Torr. & Gray) homolog of the floral homeotic gene LEAFY (PTLF), which could be used to impart male and female flower sterility, to that of three candidate attenuator-gene promoters: the cauliflower mosaic virus (CaMV) 35S basal promoter, the CaMV 35S basal promoter fused to the TMV omega element and the nopaline synthase (NOS) promoter. The promoters were evaluated via promoter::GUS gene fusions in a transgenic poplar hybrid (Populus tremula L. x P. alba L.) by both histochemical and fluorometric GUS assays. In leaves, the NOS promoter conveyed the highest activity and had a mean expression level 5-fold higher than PTLF, whereas the CaMV 35S basal promoter fused to the omega element and the CaMV 35S basal promoter alone directed mean expression levels that were 0.5x and 0.35x that of PTLF, respectively. Differential expression in shoots, leaves, stems and roots was observed only for the NOS and PTLF promoters. Strongest expression was observed in roots for the NOS promoter, whereas the PTLF promoter directed highest expression in shoots. The NOS promoter appears best suited to counteract vegetative expression of a cytotoxin driven by the PTLF promoter where 1:1 toxin:attenuator expression is required."
hella too much...... here s the index..
http://www.knockoutscience.com/articlei ... ?year=2006
the FUSA!! contaminating the bulk narcotics in every american syndicate one size fits all
Fusarium Tri4 encodes a multifunctional oxygenase required for trichothecene biosynthesis.
SP McCormick, NJ Alexander, RH Proctor
Fusarium graminearum and Fusarium sporotrichioides produce the trichothecene mycotoxins 15-acetyldeoxynivalenol and T-2 toxin, respectively. In both species, disruption of the P450 monooxygenase-encoding gene, Tri4, blocks production of the mycotoxins and leads to the accumulation of the trichothecene precursor trichodiene. To further characterize its function, the F. graminearum Tri4 (FgTri4) was heterologously expressed in the trichothecene-nonproducing species Fusarium verticillioides. Transgenic F. verticillioides carrying the FgTri4 converted exogenous trichodiene to the trichothecene biosynthetic intermediates isotrichodermin and trichothecene. Conversion of trichodiene to isotrichodermin requires seven biochemical steps. The fifth and sixth steps can occur nonenzymatically. Precursor feeding studies done in the current study indicate that wild-type F. verticillioides has the enzymatic activity necessary to carry out the seventh step, the C-3 acetylation of isotrichodermol to form isotrichodermin. Together, the results of this study indicate that the Tri4 protein catalyzes the remaining four steps and is therefore a multifunctional monooxygenase required for trichothecene biosynthesis.
You are for Ecological Restoration are you not? Also, aren't you in Vrginia? I honestly do not know but think you are. If so, could you share with us Hwy 58?
Something to do with combustion....????
To all: They say their will not be enough oxygen with in the next 25 years if the problem it "their" solutions for "our" problems are not dealt with now. Basically, it says air will be in short supply so they have to knock a few off now.
Also, TamTam, I have found nothing on the Doxy RX causing weight gane. But i did find this......
Basicaaly it says Microbes in the gut causes FAT!!!!!!!!!!!!!!!!!!!!!!!!
Dammit, I only get more seething by the minute. Hey, has Doc found the fibers content yet?
I'll go try to find the microbe/fat link for youl
She wears a plastic hat, flowered with ornaments, because her head explodes twice or three times every forty-five minutes. The marketing climate for frozen foods is snowy, she’d say while scratching her scratchiest spots. If her nails were too long her shirts and underwear sopped with what her nails uncovered beneath the skin. And if her nails were far too short, she’d plan robberies, espionage and other crafty hand driven crimes that disliked fingerprints, were ever angry at fingerprints. On Sunday nights she’d swim into the dumpsters of bookstores or behind newsstands and fill hatboxes with coupon inserts. Then, while walking home with eight or ten ribboned together boxes, she’d estimate her week’s wealth in skin and bone and muscle and nerves and fifty cents off one item coupons. Please remember, she was never much of a swimmer, not fast or very floaty. Once through her front door, she’d stumble through head explosions cutting out the most prized deals first. Those were the paper bits she used for the hourly and hemorrhaging skull breaks. Free trial offers, the buy and get after buying, were the most effective healing grafters. The closer the purchase price moved to zero the quicker they fixed what’s detonated under her plastic hat. After price the most convincing quality of any coupon are the dyes. She wasn’t concerned with the placement of colors, the appearance of foods, or the bluish happy flame of mango waterfalls forcing a room into freshness, bludgeoning away those fertile gangs of smells that rob our houses of the happy happiness we so very much want. No, she just wanted the valuable coupons under her plastic hat, inside her plastic gloves, beneath her plastic clothes. Then, on Monday morning, after stocking her clothes with enough coupons to replace a days worth of skin and explosions, she’d start walking. Her first destination was usually a warehouse style grocery store. She’d walk awkwardly through checkout lines, finding ways to wave her hands over the scanners. What began as two hundred dollars reduced to half then half once more. She found that her coupons, after becoming skin and nerve and membrane, always left their barcode behind. And that with each explosion under her hat, the life she led swam a bit deeper to the purchase price of zero.
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