Purification and characterization of six cytochrome P-450 isozymes from human liver microsomes.
Purification and characterization of six cytochrome P-450 isozymes from human liver microsomes.
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人肝微粒体中六种细胞色素 P-450 同工酶的纯化和表征。
DOI:
10.1021/bi00292a019
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发表时间:
1983
期刊:
影响因子:
2.9
通讯作者:
Guengerich,FP
中科院分区:
文献类型:
--
作者:
Wang,PP;Beaune,P;Kaminsky,LS;Dannan,GA;Kadlubar,FF;Larrey,D;Guengerich,FP
Philip P. Wang, Philippe Beaune, Laurence S. Kaminsky, Ghazi A. Dannan, FredF. Kadlubar, Dominique Larrey, and F. PeterGuengerich* abstract: Six cytochrome P-450 (P-450) isozymes were purified to electrophoretic homogeneity from the livers of four human organ donors, with three of these isozymes purified from a single individual. Differences were noted between all six P-450s for some or all of the parameters determined by the techniques of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, peptide mapping, spectral analysis of ferrous-carbon monoxide complexes, double-diffusion immunoprecipitin analysis or crossed immunoelectrophoresis (sodium dodecyl sulfate-polyacrylamide gel electrophoresis/peroxidase-coupled staining) with rabbit antisera raised to five of the P-450s, or catalytic activity toward d-benzphetamine, benzo [a] pyrene, acetanilide, debrisoquine,(J?)-and (S)-warfarin, and 1-naphthylamine. While NADPH-fortified