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Science 10 April 1987:
Vol. 236. no. 4798, pp. 188 - 190
DOI: 10.1126/science.3563495
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Articles

Science, Vol 236, Issue 4798, 188-190
Copyright © 1987 by American Association for the Advancement of Science

articles

Steroidogenesis-activator polypeptide isolated from a rat Leydig cell tumor

RC Pedersen and AC Brownie

A cycloheximide-sensitive protein responsive to adenosine 3',5'-monophosphate has been postulated to participate in the regulation of cholesterol side-chain cleavage activity in steroidogenic tissues. Such a steroidogenesis activator polypeptide (SAP) had been isolated from rat adrenocortical tissue and partially characterized. Now a polypeptide with comparable chromatographic behavior and biological activity has been purified from the rat H-540 Leydig cell tumor in quantities sufficient for amino acid sequencing. The activator contains 30 amino acid residues and has a molecular weight of 3215. The synthetic construct based on this sequence is virtually equipotent with native H-540 tumor SAP in an adrenal mitochondrial cholesterol side-chain cleavage assay. Hormonal regulation of the intracellular concentration of this activator may control the rate of cholesterol metabolism in steroidogenic organs.


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