Comparison of the multiple molecular forms of bovine adrenocortical P450scc with those of corpus luteum P450scc.
1. Bovine adrenocortical P450scc was resolved into several fractions by chromatography on AH-Sepharose 4B followed by gel filtration on Toyopearl HW55S. All fractions contained P450scc of the same molecular size and the P450scc could be resolved into 3-4 major and more than 10 minor isoelectric point forms by isoelectric focusing on polyacrylamide gel in the presence of Emulgen 913. 2. Both the AH-Sepharose chromatography profile and the isoelectric focusing pattern of the adrenocortical P450scc were more complex than those of the corpus luteum P450scc. The corpus luteum P450scc was practically devoid of the neutral to acidic isoelectric point forms. 3. Three to four P450scc subfractions with different isoelectric focusing pattern were obtained from a purified preparation of adrenocortical P450scc by ion-exchange chromatography on DEAE-Toyopearl 650S or DEAE-Sephadex A25. These P450scc subfractions showed essentially the same spectral properties, catalytic activity, molecular weight and N-terminal amino acid sequence. 4. The most acidic (the latest eluting) subfraction was composed mostly of the neutral to acidic isoelectric point forms. The sedimentation characteristics of this subfraction was also studied. 5. The structural basis of the multiple molecular forms was discussed.
Horie
S
S
Department of Biochemistry, School of Medicine, Kitasato University, Kanagawa, Japan.
Sone
Y
Y
Watanabe
T
T
Kuwada
M
M
Suzuki
H
H
Sugano
S
S
D000302:Adrenal Cortex / Q000201:enzymology*; D000818:Animals; D002417:Cattle; D002786:Cholesterol Side-Chain Cleavage Enzyme / Q000737:chemistry* / Q000302:isolation & purification; D003338:Corpus Luteum / Q000201:enzymology*; D005260:Female; D007525:Isoelectric Focusing; D007527:Isoenzymes; D008928:Mitochondria / Q000201:enzymology*
D007527:Isoenzymes; D002786:Cholesterol Side-Chain Cleavage Enzyme