Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 188-190 |
| Number of pages | 3 |
| Journal | Science |
| Volume | 236 |
| Issue number | 4798 |
| DOIs | |
| State | Published - 1987 |
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