PMID: 9187247May 23, 1997Paper

Purification and characterization of two new cytochrome P-450 related to CYP2C subfamily from rabbit small intestine microsomes

Biochimica Et Biophysica Acta
Y ShimizuM Kusunose

Abstract

Two forms of cytochrome P-450, designated P-450id and P-450ie, were purified to specific contents of 14.3 and 15.0 nmol of P-450/mg of protein, respectively, from small intestine mucosa microsomes of rabbits. P-450id and P-450ie showed apparent molecular weights of 50 and 49 kDa, respectively, on SDS-PAGE. Both P-450s catalyzed N-demethylation of nitrosodimethylamine. The NH2-terminal amino acid sequence (first 19 residues) of P-450id exhibited 74-90% identity with those of six members of the rabbit P-450 2C subfamily, except for P-450 2C3. Similarly, the NH2-terminal sequence (first 22 residues) of P-450ie showed 73-86% identity with those of the same members of the rabbit P-450 2C subfamily. The peptide mapping patterns of the two P-450s were quite different from each other. In addition, P-450id did not cross-react with the guinea-pig antibodies against P-450ie. The results indicate that rabbit small intestine mucosa contain two new distinct forms of P-450s, both of which may be classified into the 2C subfamily.

References

Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
May 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·L Spatz, P Strittmatter

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Citations

Jul 11, 2000·Japanese Journal of Pharmacology·T NakamuraY Yamazoe
Nov 2, 2007·Clinical and Experimental Pharmacology & Physiology·Man ChenHui Wang

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