银大麻哈鱼垂体胱抑素的完整氨基酸序列。

The complete amino acid sequence of pituitary cystatin from chum salmon.

作者信息

Koide Y, Noso T

机构信息

School of Fisheries Sciences, Kitasato University, Iwate, Japan.

出版信息

Biosci Biotechnol Biochem. 1994 Jan;58(1):164-9. doi: 10.1271/bbb.58.164.

DOI:10.1271/bbb.58.164

PMID:7764512

Abstract

Cystatin, a cysteine proteinase inhibitor, was isolated from chum salmon (Oncorhynchus keta) pituitary glands by ion-exchange chromatography on Mono-Q, gel filtration on Superdex 75, and reverse-phase HPLC on an ODS following ethanol-ammonium acetate extraction. Salmon pituitary cystatin was equipotent to chicken egg-white cystatin in the papain inhibitory assay. The cystatin consists of 111 amino acid residues with two disulfide linkages formed between 66-75 and 89-109, and has 43% identical sequences with chicken egg-white cystatin with consensus sequences of reactive sites, Gly(4), Gln-X-Val-X-Gly (48-52), and Ile(Val)-Pro-Trp (96-98).

摘要

胱抑素是一种半胱氨酸蛋白酶抑制剂，通过在Mono-Q上进行离子交换色谱、在Superdex 75上进行凝胶过滤以及在乙醇-醋酸铵提取后在ODS上进行反相高效液相色谱，从大麻哈鱼（Oncorhynchus keta）垂体中分离得到。在木瓜蛋白酶抑制试验中，鲑鱼垂体胱抑素与鸡卵清白蛋白胱抑素具有同等效力。该胱抑素由111个氨基酸残基组成，在66 - 75和89 - 109之间形成两个二硫键，与鸡卵清白蛋白胱抑素具有43%的相同序列，具有反应位点的共有序列Gly(4)、Gln-X-Val-X-Gly (48 - 52)和Ile(Val)-Pro-Trp (96 - 98)。