| Literature DB >> 6289278 |
Y P Loh, H A Gritsch, T L Chang.
Abstract
The biosynthesis of alpha-MSH, beta-endorphin and ACTH in the pituitary is reviewed. These neuropeptides are synthesized from a common pro-protein, pro-opiomelanocortin. The pro-protein is cleaved intragranularly, at pairs of basic residues in the molecule to yield the respective peptide products. An unique, thiol protease (pro-opiocortin converting enzyme) and a carboxypeptidase B-like enzyme, both localized within pituitary secretory granules and having a pH optimum of 5-6, appear to be involved in the proteolytic processing of pro-opiomelanocortin.Entities:
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Year: 1982 PMID： 6289278 DOI： 10.1016/0196-9781(82)90099-7
Source DB: PubMed Journal: Peptides ISSN： 0196-9781 Impact factor: 3.750