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• W7241757 abstract "Research Article1 October 1989free access Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450. W. Pyerin W. Pyerin German Cancer Research Center, Institute of Experimental Pathology, Heidelberg, FRG. Search for more papers by this author H. Taniguchi H. Taniguchi German Cancer Research Center, Institute of Experimental Pathology, Heidelberg, FRG. Search for more papers by this author W. Pyerin W. Pyerin German Cancer Research Center, Institute of Experimental Pathology, Heidelberg, FRG. Search for more papers by this author H. Taniguchi H. Taniguchi German Cancer Research Center, Institute of Experimental Pathology, Heidelberg, FRG. Search for more papers by this author Author Information W. Pyerin1 and H. Taniguchi1 1German Cancer Research Center, Institute of Experimental Pathology, Heidelberg, FRG. The EMBO Journal (1989)8:3003-3010https://doi.org/10.1002/j.1460-2075.1989.tb08450.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The major phenobarbital-inducible cytochrome P-450 purified from rat liver, a member of family II of the cytochrome P-450 gene superfamily, is rapidly phosphorylated by cAMP-dependent protein kinase. The phosphorylation reaches greater than 0.5 mol phosphate/mol P-450 after 5 min and is accompanied by a decrease in enzyme activity. The serine residue in position 128 was shown to be the sole phosphorylation site and a conformational change of the protein was indicated by a shift of the carbon monoxide difference spectrum of the reduced cytochrome from 450 to 420 nm. Comparison of amino acid sequences of various cytochrome P-450 families revealed a highly conserved arginine residue in the immediate vicinity of the phosphorylated serine residue which constitutes the kinase recognition sequence. It also revealed that only the members of the cytochrome P-450 family II carry this kinase recognition sequence. To find out whether this phosphorylation also occurs in vivo, the exchangeable phosphate pool of intact hepatocytes derived from phenobarbital-pretreated rats was labeled with 32Pi followed by an incubation of the cells with the membrane-permeating dibutyryl-cAMP or with the adenylate cyclase stimulator glucagon to activate endogenous kinase. As a result, a microsomal polypeptide with the same electrophoretic mobility as cytochrome P-450 became strongly labeled. Peptide mapping and immunoprecipitation with monospecific antibodies identified this protein as the major phenobarbital-inducible cytochrome P-450. It becomes phosphorylated at the same serine residues as in the cell-free phosphorylation.(ABSTRACT TRUNCATED AT 250 WORDS) Previous ArticleNext Article Volume 8Issue 101 October 1989In this issue RelatedDetailsLoading ..." @default.
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• W7241757 date "1989-10-01" @default.
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• W7241757 title "Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450." @default.
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• W7241757 doi "https://doi.org/10.1002/j.1460-2075.1989.tb08450.x" @default.
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