Interaction between cytochrome P450 and other drug-metabolizing enzymes: Evidence for an association of CYP1A1 with microsomal epoxide hydrolase and UDP-glucuronosyltransferase
作者： Ken-ichiro Taura , Hideyuki Yamada , Yukiko Hagino , Yuji Ishii , Masa-aki Mori
关键词: Affinity chromatography 、 Cytochrome P450 、 Sepharose 、 Bovine serum albumin 、 Enzyme 、 Molecular biology 、 Protein disulfide-isomerase 、 Microsome 、 Microsomal epoxide hydrolase 、 Biochemistry 、 Chemistry
摘要: Protein-protein interactions between cytochrome P450 (P450) and other drug-metabolizing enzymes were studied by affinity chromatography using CYP1A1-, glycine-, bovine serum albumin (BSA)-conjugated Sepharose 4B columns. Sodium cholate-solubilized microsomes from phenobarbital-treated rat liver applied to the columns material eluted with buffer containing NaCl was analyzed immunoblotting. Microsomal epoxide hydrolase (mEH) UDP-glucuronosyltransferases (UGTs), as well NADPH-P450 reductase, efficiently trapped CYP1A1 column. Glycine BSA exhibited no ability retain these proteins. Protein disulfide isomerase calnexin, non-drug-metabolizing expressed in endoplasmic reticulum, unable associate These results suggest that interacts mEH UGT facilitate a series of multistep drug metabolic conversions.
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