| Literature DB >> 206844 |
F A Opmeer, J M van Ree, D de Wied.
Abstract
The lipolytic action of natural porcine ACTH1(-39) and of a number of highly purified synthetic ACTH peptide fragments was studied using rat adipocytes. Of the analogues tested, only ACTH1(-24) exhibited full lipolytic activity with respect to intrinsic activity and affinity. Several shorter fragments appeared to be full agonists but had lower affinity. Fragments ACTH5(-10) and ACTH7(-10) were inactive. No antagonistic effects against the lipolytic action of ACTH could be demonstrated with substimulatory doses of ACTH1(-16), ACTH1(-10), ACTH7(-24) and ACTH11(-24). Based on the relative potency derived from dose-response curves, a more refined model with respect to the active centers being encoded in various sequences of the hormone, is proposed.Entities:
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Year: 1978 PMID： 206844 DOI： 10.1007/bf00586593
Source DB: PubMed Journal: Naunyn Schmiedebergs Arch Pharmacol ISSN： 0028-1298 Impact factor: 3.000