Cytochrome cobalt effect

Pretreatment with the Type I substrate, ethylmorphine, resulted in 100% mortality in both rats and mice, and aminopyrine pretreatment resulted in 100% and 64% mortality in rats and mice, respectively, exposed to disulfoton (Pawar and Fawade 1978). Nickel chloride, cobalt chloride, or cycloheximide decreased the levels of cytochrome bs, cytochrome c reductase, and total heme in rats (Fawade and Pawar 1983). These electron transport components were further decreased in rats pretreated with these inhibitors and given a single dose of disulfoton. Data from this study suggests an additive effect, since disulfoton also decreases the activities of these components. Evidence of an additive effect between disulfoton and these metabolic inhibitors was suggested by the decrease in ethylmorphine N-demethylase and acetanilide hydroxylase activities when rats were given an inhibitor followed by disulfoton. In another experiment, these inhibitors decreased the activity of delta-aminolevulinic acid synthetase, but this decrease was reversed when disulfoton was administered. 

As discussed in Sections 2.3.5 and 2.4, it is currently believed that the toxic and carcinogenic effects of PAHs are mediated by reactive diol-epoxide intermediates that interact directly with DNA and RNA, producing adducts. The formation of these adducts leads to neoplastic transformation as well as interfering with the normal functioning of rapidly proliferating tissues. As discussed above, these reactive intermediates are formed when PAHs are biotransformed by the P-450 enzymes. Interference with these metabolic pathways, by inactivation of the activated diol epoxides, reduction in tissue levels of cytochrome P-450, and direct inhibition of the cytochrome P-450 enzymes responsible for the formation of the reactive intermediates, could reduce the toxic and carcinogenic effects of PAHs. A number of drugs, such as cobaltous chloride, SKF-525-A, and 6-nitro-... 

Konorev et al. (2002) evaluated the pro- and an-tiapoptotic potential of different metalloporphyrins containing iron, cobalt, zinc, and manganese in adult rat cardiomyocytes exposed to doxorubicin. They used electron spin resonance/spin trapping and cytochrome c reduction to assess the scavenging of superoxide anion by metalloporphyrins. Superoxide anion was effectively scavenged by 5,10,... 

Trace metals, particularly copper, cobalt, and iron, greatly increase the rate of LO and influence the direction of peroxide decomposition [72], These metals function both to reduce the induction period and increase reaction rate by decomposing hydroperoxides. Trace levels of these catalysts, e.g., as little as 0.3 ppm iron or 0.01 ppm copper, will result in prooxidant effects [73]. Iron may exist in foods in the free form or as a part of an enzyme (contain organically bound haem, Fe+ or haemin, Fe+ ). Enzymes containing haematin compounds include catalase and peroxidase (plant tissues) and haemoglobin, myoglobin, and cytochrome C (animal tissues). While heat treatment results in denaturation of the enzymes, it frees the iron to greatly enhance its catalytic properties. This is particularly relevant in the formation of warmed-over off-flavor in cooked meats. 

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