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Download Cytochromes P-450 and b5 : Structure, Function, and by W. Levin, A. Y. H. Lu, D. Ryan, S. West, R. Kuntzman, A. H. PDF

By W. Levin, A. Y. H. Lu, D. Ryan, S. West, R. Kuntzman, A. H. Conney (auth.), David Y. Cooper, Otto Rosenthal, Robert Snyder, Charlotte Witmer (eds.)

P-450 has in universal with our state that it could name Phila­ delphia its native land. but there are transformations, too. The U. S. A. was once born and named during this urban. P-450 used to be first recog­ nized the following -- a strange CO-combining pigment with out relatives or func­ tion. jap employees pointed out it as an strange member of the cytochrome kin. eventually, in Philadelphia, its organic func­ tion was once tested and its progress to an international strength initiated. on the grounds that discovery of its functionality as terminal oxidase of the 21-steroid hydroxylase procedure of adrenocortical microsomes, P-450 has proved to play an analogous function in a large choice of alternative combined functionality oxidase structures concerned about biosynthesis and catabolism of particular cellphone or physique parts in addition to within the metabolism of international components coming into organisms. P-450-like oxygenating enzymes seem to be primary mobile elements in so much types of cardio organisms. Activation of molecular oxygen and incorporation of 1 of its atoms into natural compounds as cata­ lyzed by means of P-450 enzymes are reactions of significant value not just for biosynthesis and degradation of steroid hormones useful for maintaining lifestyles, but in addition for metabolic activation or inactivation of international brokers corresponding to medicinal drugs, foodstuff preservatives and ingredients, pesticides and cancer agents. in addition, P-450 associated enzyme sys­ tems can both be caused or suppressed via those brokers with major organic consequences.

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Extra resources for Cytochromes P-450 and b5 : Structure, Function, and Interaction

Example text

9th International Congress of Biochemistry, Stockholm, Abstracts, p. 341. van der Hoeven, T. , and Coon, M. J. 1974. Preparation and Properties of Partially Purified Cytochrome P-450 and NADPHcytochrome P-450 Reductase from Rabbit Liver Microsomes. J. BioI. Chern. 249: in press.

COON ET AL. 30 Analytical data on a typical purified preparation of P-450 LM are presented in Table III. A small amount of cytochrome P-420 resulting from the breakdown of P-450 was present, but no cytochrome £s could be detected. The heme content was slightly higher than would be predicted from the cytochromes present, perhaps because of the presence of heme dissociated from these proteins, and the phospholipid content of the purified cytochrome P-450 was less than one-tenth of that originally present in the microsomes.

Y. , Strobel, H. , and Coon, M. J. 1970. Properties of a solubilized form of the cytochrome P-450-containing mixed function oxidase of liver microsomes. Mol. Pharmacol. 6:213-220. Lu, A. Y. , and Conney, A. H. 1972. Reconstituted liver microsomal enzyme system that hydroxylates drugs, other foreign compounds, and endogenous substrates. II. Role of cytochrome P-450 and P-448 fractions in drug and steroid hydroxylations. J. BioI. Chern. 247:1727-1734. Nebert:JD. , Heidema, J. , Strobel, H. W. and Coon, M.

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