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2019, Ohio University, Enzo's review: "Apcalis SX 20 mg - Buy Apcalis SX online.".

In an experimen- tal setting 20 mg apcalis sx, one begins with a particular apcalis sx 20mg, dened genotype as the genetic back- ground for further analysis apcalis sx 20 mg. One then obtains single amino acid substitutions or small numbers of substitutions derived from the original background ge- notype 20mg apcalis sx. Substitutions may be obtained by imposing selective pressures such as antibodies in an experimental evolution regime or by imposing site-directed or random mutagenesis . Each of these processes relates tness to dierent kinetic aspects of surface binding . First , changes in cell binding and entry aect the performance of in- tracellular pathogens . In that gure , the substitutions 190 EA , 225 GR, and 228 SGallhavestronger binding anity than the common wild type. The fact that some substitutions raise anity suggests that binding has been adjusted by selection to an intermediate rate. It may be possible to test this idea in various experimental systems by competing viruses with dierent cell binding kinetics. Those in vitro systems allow study of competition between dierent viral genotypes (Robertson et al. It would be interesting to compare the tnesses in vivo between wild type and mutants selected for higher binding anity in vitro. The second role of substitutions arises from binding that interferes with viral tness. High anity may also ag- gregate viruses in localized regions, interfering with infectious spread. Again, it would be interesting to compete variants with dierent ani- ties under various in vitro and in vivo conditions. Receptor binding sites may also be strongly selected to avoid binding molecules similar to the host-cell receptor. For example, the nonim- mune component of horse serum attracts inuenza particles that bind the (2, 6) linkage of sialic acid (Matrosovich et al. Selection fa- vors equine inuenza strains that both bind (2, 3) linkages and avoid (2, 6) linkages. Thus, host uids or host tissues dierent from the primary infection target can cull viruses from circulation. The ki- netics of such tness losses must be balanced against kinetic gains in receptor binding and avoidance of antibodies. The third tness eect of surface substitutions arises from changes in antibody binding. A few studies have related dierent aspects of antibody-virus binding kinetics to the neutralization (killing) of viruses (Schoeld et al. This topic stands as a preliminary model for analyzing the relations between bind- ingkinetics and tness (Dimmock 1993; McLain and Dimmock 1994; Dimmock 1995). No work has clearly established the roles of various amino acid sub- stitutions in antibody neutralization kinetics. I suspect that exper- imental evolution will be an important tool in understanding the links between tness, amino acid substitutions, the kinetics of binding to host cells, and the kinetics of antibody neutralization. At equilibrium, the binding anities can also be given by the dissociation constant, Kd = 1/Ka. This may capture an important aspect of neutralization, but other pro- cesses may also be important. For example, equilibrium binding anity provides no sense of the time course of association because it describes the ratio between on-rate and o-rate. In vivo, the race occurs between the rate of antibody binding and neutralization versus the rate of patho- gen attachment and entry into host cells (Dimmock 1993; McLain and Dimmock 1994). Experimental evolution studies could be devised to measure under what conditions selection favors particular changes in rate processes or only an overall change in equilibrium anity. They measured neutralization by the rate at which amixtureofantibody and virus loses infectivity when presented with a layer of cultured host cells. Edwards and Dimmock (2000) found that, when antibodies inhibited infectivity by 50% of viruses, attachment was blocked for only 5 to 20% of viruses. Further studies demonstrated that antibody inhibition of viral fu- sion increased in proportion to neutralization. However, antibody concentration inuenced the relative contributions of blocking attach- ment versus blocking fusion: increased concentrations enhanced the degree of interference with viral attachment for bothH36andH37 an- tibodies. At high concentrations, interference with attachment became the dominant mechanism. H36 neutralized 10- fold more eciently than did H37, but H37 binding anity was 1. Pseudo-rst order kinetics typically occur for an- tibody neutralization of viruses (Dimmock 1993), although exceptions occur(McLain and Dimmock 1994). Many dierent underlying mech- anisms of reaction can give rise to pseudo-rst-order kinetics (Latham and Burgess 1977). Themost commonly proposed mechanismfor pseudo-rst-order neu- tralization follows the single-hit model, in which one assumes that a single bound antibody can neutralize a virus (Dimmock 1993). In this model, the probability at time t that a particular virion has not been hit by at least a single antibody is et,withanaveragetimeuntil the rst hit of 1/. Thelogarithmofthenumber of antibody-free virions decays linearly in time with a slope proportional to. Thisexponential decay typies models of random waiting times, random decay, and the Pois- son distribution for the number of events in a particular time period. In the antibody-virus model, one assumes an excess of antibody so that antibody pressure does not decline over time as antibodies bind to viral surfaces. In an exponential decay model of binding, there is on average one anti- body bound to each virion when t = 1, following a Poisson distribution with an average count of one. Conversely, 1 e1 = 63% neutralization predicts an average of one bound antibody per virion. The observed number of bound antibodies per virion at 63% neutral- ization varies widely (Dimmock 1993): approximately 1 for polyclonal antibodies neutralizing adenovirus hexon protein (Wohlfart 1988) and poliovirus (Wetz et al. The dierent sites have the same antigenicity but may dier in the eect of bound antibody on neutralization. Antibody bound to critical sites neutralizes; antibody bound to noncritical sites does not neutralize. Although this process does not yield a perfectly log- linear plot of neutralization versus time, the predicted kinetics are su- ciently close to log-linear (pseudo-rst-order) that departures would not be easily noticed in experimental data. Each observation (open cir- cle) shows the neutralization of a dierent inuenza strain with variant amino acids at the antibody binding site. The amino acid variants cause dierent equilibrium binding anities (Ka) with the antibody (units in l/mol). These results a suggest that neutralization dependsonquantitative eects of anity and the cumulative eects of multihit binding. The particular mechanism that leadstoquantitative eects on neu- tralization remains unclear. It may be that lower-anity antibodies pri- marily interfere with attachment to host cells by covering most viral attachment sites. By contrast, higher-anity antibodies may interfere primarily with fusion and entry to host cells, and such steric interference at the cell surface requires a lower density ofbound antibody. When virions attachtocellsurfaces,the lower-anity epitopes may lose alargerfractionofbound antibody than higher-anity epitopes. Synergism occurs when simultaneous binding by two antibodies causes higher neutralization than expected by adding the eects of each anti- body when bound alone. Thus, the tness eect of an amino acid sub- stitution may depend both on the reduced anity fortheconforming antibody and on the context of other antibody-epitope combinations for that pathogen genotype. Structural studies locate particular amino acid sites in their three-dimensional context. Experimental evolution substitutes amino acids in response to immune pressure, altered cellular receptors, in- terference with the viral receptor binding site, or changed kinetics that arise in cell culture. Binding anity and kinetics ofneutralization relate amino acid substitutions to components of tness. In this section, I briey list a few additional studies of experimental evolution. Experimental deletion of the B cell response led to an absence of aminoacidsubstitutions in the presumed antibody epitopes, demonstrating that substitutions in surface proteins arise in response to antibodies rather than cell tropism. Not surprisingly, escape mutants do arise frequently with amino acid substitutions in the immunodominant surface antigens (Gow and Mutimer 2000). Antigenic change in response to antibody pressure can change polymerase function, and substitutions in the polymerase in re- sponse to nucleoside analog drugs canchange antigenic properties of surface proteins. The mapping of amino acidsubstitutions to tness may be rather complex in this case. Amino acid substitutions in measles hem- agglutinin appear to alter both antigenicity and neurovirulence. Measles virus also appears to change its binding anity for dierent cellularreceptors during adaptation to cell culture (Nielsen et al. The amino acid changes associated with receptor anity occur in the surface hemagglutinin protein. Thelife cycle of arthropod-borne viruses (arboviruses) typically al- ternates between vertebrate hosts and blood-feeding arthropod vectors. However, many stud- ies have reported a high degree of antigenic conservation and slow rates of molecular evolution (reviewed byCooper and Scott 2001). Cooper and Scott (2001) used experimental evolution to study how alternating hosts potentially constrain adaptive change. They passaged viral lineages in cell culture through either mosquito cells only, avian cells only, or alternating between mosquito and avian cells. They then measured various characteristics of infectivity and growth on insect, avian, or mammalian host cells. The dierent passage histories produced signicant dierences in in- fectivity and growth between the lineages. The lineages that alternated between the two host types expressedintermediatephenotypes rela- tive to those lineages passaged only in one cell type. Fur- ther experimental evolutionstudiesinvivo may provide more insight into how multiple selective pressuresconstraintherateofevolutionary change. Those variants provide material for a rapid response to new or chang- ing selective pressures. The consequences of varying population size on the rate of adaptation have been analyzed under controlled experi- mental conditions. Afewbacterial studies analyzed escape mutants in response to con- trolledantibody pressure (e. Other scattered studies of experimental evolution have been done on nonviral pathogens, but none approaches thescope of the viral experiments. The rst infection of a host initially stim- ulates the naive IgM antibody repertoire, which has relatively low anity and broad specicity. The mature, high-anity antibody response de- velops by various processes, including competition between antibodies based on binding anity. Apathogengains if its most highly antigenic sites have low rates of neutralization or high rates of antigenic change. Highly antigenic de- coy sites can draw antibody pressure away from sites more sensitive to neutralization or more strongly constrained against change because of essential function. Theimmunodominant sites draw the maturing repertoire away from the binding pocket. To what extent have immunodominant sites evolved to draw antibody pressure away from more sensitive sites? This is a dicult question, because immunodominant sites may happen to be away from receptor binding pockets or other functional sites for a variety of reasons. No experimental systems developed so far provide a clear way to ad- dress this problem. One needs experimental control of initial antibody pressure and a feedback mechanism that enhances antibody pressure on epitopes with stronger antibody binding. Feedback favors epitopes with relatively lower rates of neutralization to evolve relatively stronger antibody binding. Such decoy sites might additionally be favored if they could tolerate a broad array of amino acid escape mutants. This sort of experimental evolution would provide clues about the forces that have shaped immunodominance. Mathematical models of immunodominance such as those developed by Nowak and May (2000) would aid in designing experiments and clarifying evolutionary process. These experiments could be repeated, starting with geno- types that have dierent amino acid substitutions at varying distances from site 226. It would be interesting to know the pleiotropic consequences of antibody escape mutants for other components of t- ness, such as binding to host receptors, growth rate, and virulence. A study that matched amino acid substitutions to kinetic pro- cesses would illuminate the mechanistic basis of tness and provide insight into the microevolutionary patterns of change in proteins. Those isolates can be grown in vivoinmiceandother hosts, but the change in hosts compromises interpretations of kinetics and tness. It would be interesting to develop an experimental model of inuenza A in aquatic birds,theancestralhostforthisvirus. This would allow study of natural variation in avian isolates coupled with in vivo experimental analysis of tness components.

However apcalis sx 20 mg, the energy required to distort the conformation of the mutant epitope during binding reduced the binding anity of theantibody by 4 apcalis sx 20mg,000-fold relative to the anity of the antibody for the original type 20 mg apcalis sx. These various studies of antibody binding 20mg apcalis sx, structure , and kinetics provide necessary background for analyses of evolutionary change at the amino acid level . Sialic acid components of host cells form the primary site of inuenza attachment . This function seems to aid in releasing progeny viral particles from infected host cells . It may be that viruses lacking neuraminidase activity enter host cells and replicate , but get stuck on the surface of the cell by attachment to sialic acid (Palese and Compans 1976) . First, surface mapping determines which amino acids occur in sites accessible to antibodies. Statistical methods identied which changed amino acids caused a reduction in antibody binding. There are some problems with inferring antibody pressure by map- ping surface antigenicity. Dierent natural and laboratory isolates of inuenza may have multiple amino acid dierences. This makes it dif- cult to assign changed antibody binding either to single amino acid substitutions or to the role of the genetic background with variations at other sites. In addition, changed antibody binding at dierent sites may have dierent consequences for binding kinetics and viral tness. The locations of the escape variants map the potentially variable sites that can mutate to avoid recognition while preserving the ability to remain infectious. This antigenic map can be used to determine whether nat- urally varying amino acid sites likely changed under antibody pressure or by some other process. These alternatives can be tested by site-directed mutagen- esis, which experimentally changes particular amino acids. Athirdexperimental technique simultaneously applies antibodies to twoormoresites (Yewdell et al. This mimics host reactions in which two or more immunodominant sites gen- erate neutralizing antibodies. The frequency of escape mutants to a sin- gle antibody is about 105,sosimultaneous escape against two distinct antibodies occurs at a vanishingly low frequency of 1010. Itappears that host antibodies directed simultaneously to two or more sites can greatly reduce the chance of new escape mutants during the course of asingleinfection. Afourthexperimental method focuses on escape mutants from low- anity, subneutralizing antibodies (Thomas et al. Clearance and protection probably derive from high-anity IgA and IgG antibodies rather than low-anity IgM. This study does, however, call attention totheprocesses by which immunodominance develops within a host. The stronger antigenic sites apparently out- compete weaker sites in attracting high-anity antibodies. Sialic acid occurs as the terminal residue attached to galactose on certain carbohydrate side chains. Two commonlinkagesbetween sialic acid and galactose occur in natural molecules, the (2, 3) and (2, 6) forms. The binding site apparently evolved before the evolution of the dierent subtypes and has been retained during subsequent divergence. The human inuenza A subtypes H1, H2, and H3 derived from avian ancestors (Webster et al. Each human subtype evolved from the matching subtype in aquatic birds, for example, human H1 from avian H1. In all three subtypes, the binding anity of human lineages evolved to favor the (2, 6) linkage (Paulson 1985; Rogers and DSouza 1989; Connoretal. The evolutionary pathways dier for the human subtypes with regard to the amino acid substitutions and changes in binding that eventually led to preference for the (2, 6) form. Human sub- types H2 and H3 have substitutions at positions 226 and 228 relative to avian ancestors. Thus, dierent human lineages have followed dierent pathways of adaptation to receptor binding. Horse serum contains (2, 6)-linked sialic acid, which binds to human strains of inuenza and interferes with the viral life cycle. The horse serum therefore selects strongly foraltered binding to (2, 3)-linked sialic acid (Matrosovich et al. This substitution changed the leucine of human H3 to a glutamine residue, the same residue found in the ancestral avian H3 subtype. This substitution caused the modi- ed virus to avoid (2, 6) binding and interference by horse serum and allowed binding to (2, 3)-bearing receptors as in the ancestral avian type. They began with aduckH3isolate that had glutamine at position 226 and favored bind- ing to (2, 3) sialic acid linkages. This selection process caused replacement of glutamine at position 226 by leucine, which inturnfavoredbindingof(2, 6)-over(2, 3)-linked sialic acid. If selection of avian H1 for a change from (2, 3) to (2, 6) binding causes the same substitutions as occurred in the human H1 lin- eage, then the dierent genetic background of avian H1 compared with H3 would be implicated in shaping the particular amino acid substitu- tions. By contrast, if experimental evolution favors a change at posi- tion 226 as in H3, then the evolution of human H1 receptor binding may have followed a more complex pathway than simple selection for (2, 6)-linked sialic acid. Various steps have been proposed for adaptation of aquatic bird iso- latestohumans. These studies raise the general problem of evolutionary pathways by which pathogens change host receptors. If two or more pathogen func- tions must change simultaneously, then changes in receptor anity may be rare. The need for joint change may cause signicant constraint on amino acid substitutions in receptor binding factors. In an experimen- tal setting, one begins with a particular, dened genotype as the genetic back- ground for further analysis. One then obtains single amino acid substitutions or small numbers of substitutions derived from the original background ge- notype. Substitutions may be obtained by imposing selective pressures such as antibodies in an experimental evolution regime or by imposing site-directed or random mutagenesis. Each of these processes relates tness to dierent kinetic aspects of surface binding. First, changes in cell binding and entry aect the performance of in- tracellular pathogens. In that gure, the substitutions 190 EA, 225 GR, and 228 SGallhavestronger binding anity than the common wild type. The fact that some substitutions raise anity suggests that binding has been adjusted by selection to an intermediate rate. It may be possible to test this idea in various experimental systems by competing viruses with dierent cell binding kinetics. Those in vitro systems allow study of competition between dierent viral genotypes (Robertson et al. It would be interesting to compare the tnesses in vivo between wild type and mutants selected for higher binding anity in vitro. The second role of substitutions arises from binding that interferes with viral tness. High anity may also ag- gregate viruses in localized regions, interfering with infectious spread. Again, it would be interesting to compete variants with dierent ani- ties under various in vitro and in vivo conditions. Receptor binding sites may also be strongly selected to avoid binding molecules similar to the host-cell receptor. For example, the nonim- mune component of horse serum attracts inuenza particles that bind the (2, 6) linkage of sialic acid (Matrosovich et al. Selection fa- vors equine inuenza strains that both bind (2, 3) linkages and avoid (2, 6) linkages. Thus, host uids or host tissues dierent from the primary infection target can cull viruses from circulation. The ki- netics of such tness losses must be balanced against kinetic gains in receptor binding and avoidance of antibodies. The third tness eect of surface substitutions arises from changes in antibody binding. A few studies have related dierent aspects of antibody-virus binding kinetics to the neutralization (killing) of viruses (Schoeld et al. This topic stands as a preliminary model for analyzing the relations between bind- ingkinetics and tness (Dimmock 1993; McLain and Dimmock 1994; Dimmock 1995). No work has clearly established the roles of various amino acid sub- stitutions in antibody neutralization kinetics. I suspect that exper- imental evolution will be an important tool in understanding the links between tness, amino acid substitutions, the kinetics of binding to host cells, and the kinetics of antibody neutralization. At equilibrium, the binding anities can also be given by the dissociation constant, Kd = 1/Ka. This may capture an important aspect of neutralization, but other pro- cesses may also be important. For example, equilibrium binding anity provides no sense of the time course of association because it describes the ratio between on-rate and o-rate. In vivo, the race occurs between the rate of antibody binding and neutralization versus the rate of patho- gen attachment and entry into host cells (Dimmock 1993; McLain and Dimmock 1994). Experimental evolution studies could be devised to measure under what conditions selection favors particular changes in rate processes or only an overall change in equilibrium anity. They measured neutralization by the rate at which amixtureofantibody and virus loses infectivity when presented with a layer of cultured host cells. Edwards and Dimmock (2000) found that, when antibodies inhibited infectivity by 50% of viruses, attachment was blocked for only 5 to 20% of viruses. Further studies demonstrated that antibody inhibition of viral fu- sion increased in proportion to neutralization. However, antibody concentration inuenced the relative contributions of blocking attach- ment versus blocking fusion: increased concentrations enhanced the degree of interference with viral attachment for bothH36andH37 an- tibodies. At high concentrations, interference with attachment became the dominant mechanism. H36 neutralized 10- fold more eciently than did H37, but H37 binding anity was 1. Pseudo-rst order kinetics typically occur for an- tibody neutralization of viruses (Dimmock 1993), although exceptions occur(McLain and Dimmock 1994). Many dierent underlying mech- anisms of reaction can give rise to pseudo-rst-order kinetics (Latham and Burgess 1977). Themost commonly proposed mechanismfor pseudo-rst-order neu- tralization follows the single-hit model, in which one assumes that a single bound antibody can neutralize a virus (Dimmock 1993). In this model, the probability at time t that a particular virion has not been hit by at least a single antibody is et,withanaveragetimeuntil the rst hit of 1/. Thelogarithmofthenumber of antibody-free virions decays linearly in time with a slope proportional to. Thisexponential decay typies models of random waiting times, random decay, and the Pois- son distribution for the number of events in a particular time period. In the antibody-virus model, one assumes an excess of antibody so that antibody pressure does not decline over time as antibodies bind to viral surfaces. In an exponential decay model of binding, there is on average one anti- body bound to each virion when t = 1, following a Poisson distribution with an average count of one. Conversely, 1 e1 = 63% neutralization predicts an average of one bound antibody per virion. The observed number of bound antibodies per virion at 63% neutral- ization varies widely (Dimmock 1993): approximately 1 for polyclonal antibodies neutralizing adenovirus hexon protein (Wohlfart 1988) and poliovirus (Wetz et al. The dierent sites have the same antigenicity but may dier in the eect of bound antibody on neutralization. Antibody bound to critical sites neutralizes; antibody bound to noncritical sites does not neutralize. Although this process does not yield a perfectly log- linear plot of neutralization versus time, the predicted kinetics are su- ciently close to log-linear (pseudo-rst-order) that departures would not be easily noticed in experimental data. Each observation (open cir- cle) shows the neutralization of a dierent inuenza strain with variant amino acids at the antibody binding site. The amino acid variants cause dierent equilibrium binding anities (Ka) with the antibody (units in l/mol). These results a suggest that neutralization dependsonquantitative eects of anity and the cumulative eects of multihit binding. The particular mechanism that leadstoquantitative eects on neu- tralization remains unclear. It may be that lower-anity antibodies pri- marily interfere with attachment to host cells by covering most viral attachment sites. By contrast, higher-anity antibodies may interfere primarily with fusion and entry to host cells, and such steric interference at the cell surface requires a lower density ofbound antibody. When virions attachtocellsurfaces,the lower-anity epitopes may lose alargerfractionofbound antibody than higher-anity epitopes. Synergism occurs when simultaneous binding by two antibodies causes higher neutralization than expected by adding the eects of each anti- body when bound alone. Thus, the tness eect of an amino acid sub- stitution may depend both on the reduced anity fortheconforming antibody and on the context of other antibody-epitope combinations for that pathogen genotype. Structural studies locate particular amino acid sites in their three-dimensional context.

This could lead to acetoacetate buildup 20mg apcalis sx, namely ketonuria and possibly a block in fat utilization of even numbered carbon atoms apcalis sx 20 mg, leaving odd numbered carbons to predominate 20 mg apcalis sx. With this much harm coming from malonic acid apcalis sx 20mg, why have we not noticed this as we eat malonate-containing food? Fortunately , the list of malonate-free foods is much longer than malonate-containing foods . Malonate-Free Foods Here is the malonate-free food list; stick to it; do not eat foods that are not listed . The fastest way to recover the health of your sick organ , is to stop poisoning it with malonic acid . You may notice less sleepiness after eating and a higher body temperature after a few weeks , which brings with it a rosier complexion. Eat Only These Remember, that a food may be malonate-free and still not be good for you for other reasons. But milk from the su- permarket (not including goat milk) is an exception; it has traces. Yet, cows milk (based on 2 samples) directly from the cow did not have malonic acid, either. Your 21 Day Program does not allow any dairy foods, though, not even with treatment. Yet, it has never been suspected that we are eating it daily in significant amounts! Does the tumor attract it the way a rapidly divid- ing tissue attracts metal or carcinogens? Or does the metal al- ready piled up in the tumor cells attract the malonate because of its chelating nature? Perhaps malonate accumulates in tumor cells simply because it cannot be detoxified there. I believe there is a normal route for your body to metabolize malonic acid, because when malonic acid-containing foods are eaten, I observe the immediate appearance of malonyl- Coenzyme A (malonyl CoA). Malonyl CoA has been well studied by scientists and found to be the beginning of fat formation. So this alternate fat-making mechanism that uses up malonic acid seems to me like a favor evolution is trying to do for us. Its normal ability to metabolize malonic acid is lost, so it must try the next route, detoxification. Detoxifying Malonate A popular detoxification method used by the body is to pin a methyl group onto the offending molecule. That uses up the or- gans supply of vitamin B12 and folic acid, but at least the malo- nic acid is gone. Of course we must still get rid of the methyl malonate, which is toxic, but thats another story. Another drawback of pinning a methyl group is that it uses up your methyl supply, which means methionine, choline and betaine. The organ under siege is becoming vitamin deficient and malnourished, and so is the rest of your body that is trying to support it by sending more supplies to it. If it has a tough, thick wall around it, these supplements cannot enter, so we must wait for the second week of the 21 Day Program. There are three more steps: malonic acid methyl malonate maleic acid D-malic acid maleic anhydride Fig. Tumor cells have lost the ability to do the detoxifying chemistry on their own, but if you supply the ingredients, they can still carry out the detoxification routine. Couldnt we simply stay on these supplements and not be deprived of the malonate-containing foods? Unfortunately, we would have to stay drenched in supplements, even taking them in the night. Other Malonic Acid Sources Once I identified malonic acid as a common denominator in all tumors I searched everywhere for it. Then most recently I learned that acrylic acid that we eat with heated oils gets changed into malonic acid by our metabolism. You have killed tapeworms, removed dental plastic, and are in the process of excluding it from your diet. Some Expected Benefits The most surprising benefit from the malonate-free diet and malonate-free mouth is stopping the production of effusates. Effusates are caused by seepage of body fluid into places where it does not belong. The lung is a favorite tissue for water ac- cumulation of this type, but the abdomen is another common site. The actual culprit is maleic anhydride a substance that is formed from malonic acid in your body. Maleic anhydride as a cause of tissue edema has been 67 known a very long time, but only when inhaled. It was never guessed that cancer sufferers with effusions actually had this chemical in them. And the pressure of this fluid against heart and lungs, against liver and intestine, or against lymph nodes in the groin can produce se- vere pain and breathlessness. Another surprising benefit of removing all malonate from your body is improved kidney function. Stopping use of malonic acid foods and getting every vestige of plastic out of your mouth can start your 67 The Merck Index, 10th Ed. But eating the tiniest bit of an ordinary malonate- containing dairy product (not allowed in this program) can ruin your progress in days! No amount of the detoxifiers, vitamins B12, C and folic acid could stop effusates from occurring or creatinine levels from rising when malonates were still arriving in the body from any source. We were forced to conclude that detoxifying malonic acid after consuming it did not prevent the damage done by it. The supplements needed to detoxify all the malonates in your body are included in the 21 Day Program. In a few days, with your new malonate-free diet and rein- forcing supplements, your tumor cells will no longer have to put up with Krebs cycle blockage. And a daily dose of thyroid will help your mitochondria to divide so fresh young mitochondria are born to handle the improved Krebs cycle activity. Damaging Dyes Your anti-tumor (tumor-shrinking) diet should also be free of carcinogenic dyes. Of course, we have believed that our diet is free of cancer-causing dyes, since laws were passed outlawing them decades ago. Cheese, butter, cream, which state that an- natto seed or riboflavin (natural dyes) have been added, also have traces of these dyes! Not only these, but a host of azo dyes, a finding as unbelievable as it is revealing. Azo dyes have a special chemical structure that involves two nitrogen atoms ( N=N). Is it the result of an error in identifying it to the manufacturer using other food dyes? A manufacturer using unsafe dye for some legitimate purpose and safe food dye nearby cannot keep them totally apart? One cannot expect the work force in a fac- tory to understand the issuesthe terrible seriousness of keep- ing them apartthe system must be made fool proof. With over 20,000,000 people (mostly women) dying their hair in the United States alone, should it not be made safe? Could there be simple negligence, in spite of safeguards such as required testing of each batch of synthetic dye to be used? This would proba- bly uncover the mysterious transmissible factor that pollutes nearly all (over 90%) of the processed food in the U. It was a cruel hoax to perpetrate on young war heroes and their families, but incredibly, researchers 71 are still experimenting with its use! It is not easily detoxified by your body and therefore, cannot be quickly eliminated. The left hand portion of the molecule is respon- sible for the carcinogenic action. It produces mainly tumors of the liver, gallbladder, lung, and urinary blad- der (particularly papillomas here). Most azo dyes were taken out of the food market because of their carcinogenicity but now are present everywhere in trace amounts, detected by the Syncrometer. At one time it was allowed as a butter colorant, hence its popular name Butter Yellow. It has three azo portions in the molecule, making it the most difficult of dyes to detoxify, too. While it is concentrated inside the tumor, it slowly leaks out, being taken up by the liver and other vital organs. It requires large doses of coenzyme Q10, vitamin B2 and glutathione (this is part of the 21 Day Program) to detoxify our azo dye collection. When we track carcinogenic dyes with the Syncrometer, we see them appear in the kidneys and bladder afterward. Hair dye and food dye are considered to be far apart in terms of danger to the body by our government agencies. It is assumed that the hair, being external to the body, does not transmit its dye or other chemicals to the body. Hair dye is immediately absorbed by the scalp and remains there in a large reservoir to be slowly absorbed for six weeks! For this rea- son, hair dye should be non-carcinogenic and easily excreted by the body. If you have used hair dye you must begin to detoxify it and use only all-herbal dye in the future (see Sources). Even eggplants and bananas are colored, suggesting a combination of pesticide and dye was used. Fast Green brings with it the lanthanide metals (thulium, gadolinium, lanthanum, etc. Two hot water washes are needed to clean the surface enough to risk cutting the fruit. Remember, wherever the lanthanides arrive in your body, immunity is im- mediately dropped. This allows parasite eggs to survive, as well as Streptococcus bacteria, the pain causers. The lanthanides polluting this dye could be the way children initiate cancers even when they do not have tooth fillings. A mutation at these genes could result from a translocation similar to The Philadelphia Chromosome, characteristic of leukemia, a bone marrow cancer. At the bone marrow the Syncrometer detects abnormal vitamin A products like 13-cis-retinoic acid instead of the normal 9-cis. These vitamin A members are probably important in the growth regulation for which vitamin A is known. This could also explain why vitamin A, given to cancer patients, was found to inhibit tumor formation many times in the past. Now you must pay closer attention to natural food to be sure it has not been dyed. By avoiding all dairy products besides processed foods and washing natural foods 75 Rettura, G. This is the main reason for removing dairy products from the diet during the 21 Day Program. After your tumors are gone and health has returned, you can begin to detoxify food dyes by adding vitamin B2 to the food itself. Dont Eat Carcinogenic Metals Even though our bodies need copper, cobalt, germanium and perhaps even vanadium, it is needed in organic form. Certainly, the body has detoxification mechanisms, but these use up your glutathione and precious metabolites. Although the body can often make the organic form out of inorganic metal that you eat, this does not justify eating it. Perhaps the practice of grounding the house electricity is partly to blame for so much corro- sion. This is very dif- ficult to achieve, since even dust carries bacteria and fungal spores. A manu- facturer is very tempted to overdo the antiseptic, for your pro- tection and their legal protection. In fact, what is required is a thorough drenching of bins without 82 rinsing or drying. The cancer patient must have no isopropyl alcohol which is the most common antiseptic. For this supremely compelling reason the cancer patient must not eat bottled, canned, or pack- aged food (with a few exceptions as noted in this book). Although the pesticide has a specific chemical that is the active ingredient, this is usually just a few percent. Over half of all the greens (lettuce, spinach, parsley) on supermarket shelves that I tested were positive for benzene, implicating pes- ticide. Organic produce was only slightly better, testing negative only if in its original plastic package. It is sad for the vegetarian especially, and those health-minded individu- als who promote juice-making, raw vegetables, and a natural diet.

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