一种人垂体糖肽的完整氨基酸序列：促肾上腺皮质激素原的一种重要成熟产物。
Complete amino acid sequence of a human pituitary glycopeptide: an important maturation product of pro-opiomelanocortin.
作者信息
Seidah N G, Chrétien M
出版信息
Proc Natl Acad Sci U S A. 1981 Jul;78(7):4236-40. doi: 10.1073/pnas.78.7.4236.
Abstract
A glycopeptide isolated in relatively large amounts from human pituitary glands was completely purified, and its sequence was determined. The primary sequence represents the NH2-terminal 76 amino acid residues of pro-opiomelanocortin (POMC). This important secretory product of POMC was shown to possess an interesting aldosterone-stimulating activity on a human adrenal aldosteronoma. It is O-glycosylated at Thr-45 and N-glycosylated at Asn-65. Only one sequence variation with the human genomic DNA was found. Furthermore, comparison with the other preferred cleavage sites of human POMC reveals that the pair of basic residues Lys-Arg represents the major sites of enzymatic maturation of this precursor molecule. This predicts a highly specific type of enzyme involved in the maturation of POMC in the anterior lobe of the human pituitary.
摘要
从人垂体中大量分离得到的一种糖肽被完全纯化，并测定了其序列。一级序列代表促肾上腺皮质激素原（POMC）的氨基末端76个氨基酸残基。POMC的这种重要分泌产物对人肾上腺醛固酮瘤具有有趣的醛固酮刺激活性。它在苏氨酸-45处进行O-糖基化，在天冬酰胺-65处进行N-糖基化。与人类基因组DNA仅发现一个序列变异。此外，与人类POMC的其他优选切割位点比较表明，碱性残基赖氨酸-精氨酸对代表了该前体分子酶促成熟的主要位点。这预示着一种高度特异性的酶参与人垂体前叶POMC的成熟。
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Proc Natl Acad Sci U S A. 1981 Jul;78(7):4236-40. doi: 10.1073/pnas.78.7.4236.
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