AMINO-ACID-SEQUENCE AND LOCATION OF THE DISULFIDE BONDS IN BOVINE BETA-2 GLYCOPROTEIN-I - THE PRESENCE OF 5 SUSHI DOMAINS

被引：134

作者：

KATO, H

ENJYOJI, K

机构：

[1] National Cardiovascular Center Research Institute, Suita, Osaka 565

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 50期

关键词：

D O I：

10.1021/bi00114a012

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：11687 / 11694

页数：8

共 18 条

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