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牛β2糖蛋白I的氨基酸序列和二硫键位置:存在五个寿司结构域。

Amino acid sequence and location of the disulfide bonds in bovine beta 2 glycoprotein I: the presence of five Sushi domains.

作者信息

Kato H, Enjyoji K

机构信息

National Cardiovascular Center Research Institute, Osaka, Japan.

出版信息

Biochemistry. 1991 Dec 17;30(50):11687-94. doi: 10.1021/bi00114a012.

Abstract

beta 2 glycoprotein I is a plasma protein with the ability to bind with various kinds of negatively charged substances. The complete amino acid sequence and the location of all the disulfide bonds of bovine beta 2 glycoprotein I were determined. Bovine beta 2 glycoprotein I consists of 326 amino acid residues with five asparagine-linked carbohydrate chains. Homology with the human protein was calculated to be 83%. Eleven disulfide bonds in bovine beta 2 glycoprotein I constitute four characteristic domains, Sushi domains, and one modified form of a Sushi domain.

摘要

β2糖蛋白I是一种血浆蛋白,能够与各种带负电荷的物质结合。已确定牛β2糖蛋白I的完整氨基酸序列和所有二硫键的位置。牛β2糖蛋白I由326个氨基酸残基组成,带有五条天冬酰胺连接的碳水化合物链。计算得出与人类蛋白质的同源性为83%。牛β2糖蛋白I中的11个二硫键构成了四个特征结构域,即寿司结构域,以及一个改良形式的寿司结构域。

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