PHOSPHORYLATION OF CYTOCHROME P-450(SCC) BY PROTEIN-KINASE-C - PROTECTIVE EFFECTS OF ADRENODOXIN AND CYTOCHROME B(5)

Authors
LOBANOV NA HENSEY CE USANOV SA AZZI A
Citation
Na. Lobanov et al., PHOSPHORYLATION OF CYTOCHROME P-450(SCC) BY PROTEIN-KINASE-C - PROTECTIVE EFFECTS OF ADRENODOXIN AND CYTOCHROME B(5), Biochemistry, 58(10), 1993, pp. 1118-1124
Citations number
24
Categorie Soggetti
Biology
Journal title
Biochemistry → ACNP
ISSN journal
00062979
Volume
58
Issue
10
Year of publication
1993
Pages
1118 - 1124
Database
ISI
SICI code
0006-2979(1993)58:10<1118:POCPBP>2.0.ZU;2-F
Abstract
Cholesterol-hydroxylating cytochrome P-450 (P-450(scc)) from bovine ad renocortical mitochondria is phosphorylated by protein kinase C. Analy sis is of products of proteolytic modification of phosphorylated cytoc hrome P-450(scc) suggests that phosphorylated amino acid residues are localized in its N-terminal region. Preincubation of cytochrome P-450( scc) with adrenodoxin or cytochrome b(5) decreases the amount of phosp hate incorporated into cytochrome P-450(scc). This effect depends on p rotein concentration.