| http://purl.uniprot.org/citations/2583091 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
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| http://purl.uniprot.org/citations/2583091 | http://www.w3.org/2000/01/rdf-schema#comment | "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)"xsd:string |
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| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/author | "Taniguchi H."xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/author | "Taniguchi H."xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/author | "Pyerin W."xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/author | "Pyerin W."xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/date | "1989"xsd:gYear |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/date | "1989"xsd:gYear |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/pages | "3003-3010"xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/pages | "3003-3010"xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/title | "Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450."xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/title | "Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450."xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/volume | "8"xsd:string |
| http://purl.uniprot.org/citations/2583091 | http://purl.uniprot.org/core/volume | "8"xsd:string |
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| http://purl.uniprot.org/uniprot/P00176 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/2583091 |