Purification and comparative characterization of cytochrome P-450scc from porcine adrenocortical mitochondria.
Cytochrome P-450scc (cholesterol side-chain cleavage enzyme) was purified from porcine adrenocortical mitochondria. 2. The purified cytochrome P-450scc was found to be homogeneous on SDS-polyacrylamide gel electrophoresis. 3. The heme content of the purified enzyme was 20.6 nmol/mg protein. 4. The enzymatic activity of the reconstituted cytochrome P-450scc-linked monooxygenase system amounted to 7.8 nmol of pregnenolone formed per nmole of P-450 per minute, with cholesterol as a substrate. 5. The amino acid sequence of the amino-terminal region of the cytochrome P-450scc and the amino acid residue at the carboxyl terminal were determined and compared with those of other mammalian cytochromes P-450scc.
Iwahashi
K
K
Department of Biochemistry, Kagawa Medical School, Japan.
Tsubaki
M
M
Miyatake
A
A
Ichikawa
Y
Y
D000302:Adrenal Cortex / Q000201:enzymology* / Q000648:ultrastructure; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002784:Cholesterol / Q000378:metabolism; D002786:Cholesterol Side-Chain Cleavage Enzyme / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016415:Sequence Alignment; D013552:Swine
D000596:Amino Acids; D002784:Cholesterol; D002786:Cholesterol Side-Chain Cleavage Enzyme