绿海龟催乳素的完整氨基酸序列。

The complete amino acid sequence of prolactin from the sea turtle (Chelonia mydas).

作者信息

Yasuda A, Kawauchi H, Papkoff H

机构信息

Laboratory of Molecular Endocrinology, School of Fisheries Sciences, Kitasato University, Iwate, Japan.

出版信息

Gen Comp Endocrinol. 1990 Dec;80(3):363-71. doi: 10.1016/0016-6480(90)90185-o.

DOI:10.1016/0016-6480(90)90185-o

PMID:2289679

Abstract

The complete amino acid sequence of prolactin (PRL) from a reptile, the sea turtle (Chelonia mydas), was determined for the first time. Sequence analysis was performed on fragments obtained from cleavage of intact and performic acid-oxidized hormone with lysyl endopeptidase, Staphylococcus aureus protease, and o-iodosobenzoic acid employing manual Edman degradation. The sea turtle PRL consists of 198 amino acid residues with three disulfide linkages formed between residues 4-11, 58-173, and 190-198 and possesses heterogeneity indicated by four replacements at positions 55, 145, 148, and 171. Sequence comparison with other vertebrate PRLs revealed that the degree of sequence identity conforms well to expectations based on phylogeny except for the rodent PRLs; sea turtle PRL has 86% identity with chicken PRL; 81% with horse, pig, and fin whale PRLs; 75-71% with cattle, sheep, and human PRLs; 60-56% with mouse and rat PRLs; and 35-31% with carp, salmon, and tilapia PRLs.

摘要

首次测定了一种爬行动物——绿海龟（蠵龟）催乳素（PRL）的完整氨基酸序列。使用手动埃德曼降解法，对用赖氨酰内肽酶、金黄色葡萄球菌蛋白酶和邻碘苯甲酸切割完整的和过甲酸氧化的激素所获得的片段进行了序列分析。绿海龟PRL由198个氨基酸残基组成，在第4 - 11、58 - 173和190 - 198位残基之间形成了三个二硫键，并且在第55、145、148和171位有四处替换，表现出异质性。与其他脊椎动物PRL的序列比较表明，除了啮齿动物的PRL外，序列同一性程度与基于系统发育的预期非常吻合；绿海龟PRL与鸡PRL有86%的同一性；与马、猪和长须鲸的PRL有81%的同一性；与牛、羊和人PRL有75 - 71%的同一性；与小鼠和大鼠PRL有60 - 56%的同一性；与鲤鱼、鲑鱼和罗非鱼PRL有35 - 31%的同一性。