Loh Y P, Gritsch H A, Chang T L
Peptides. 1982 May-Jun;3(3):397-404. doi: 10.1016/0196-9781(82)90099-7.
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.
本文综述了垂体中α-促黑素(α-MSH)、β-内啡肽和促肾上腺皮质激素(ACTH)的生物合成。这些神经肽由一种共同的前体蛋白——阿黑皮素原合成。该前体蛋白在分子内成对的碱性残基处进行颗粒内切割,以产生相应的肽产物。一种独特的硫醇蛋白酶(阿黑皮素原转换酶)和一种类羧肽酶B,均定位于垂体分泌颗粒内,最适pH为5 - 6,似乎参与了阿黑皮素原的蛋白水解加工过程。