LOCATION OF THE DISULFIDE BONDS IN HUMAN PLASMA PREKALLIKREIN - THE PRESENCE OF 4 NOVEL APPLE DOMAINS IN THE AMINO-TERMINAL PORTION OF THE MOLECULE

被引：73

作者：

MCMULLEN, BA ^{[1
]}

FUJIKAWA, K ^{[1
]}

DAVIE, EW ^{[1
]}

机构：

[1] UNIV WASHINGTON,DEPT BIOCHEM,SEATTLE,WA 98195

来源：

BIOCHEMISTRY | 1991年 / 30卷 / 08期

关键词：

D O I：

10.1021/bi00222a007

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：

The location of 16 of the 18 disulfide bonds in human plasma prekallikrein was determined by amino acid sequence analysis of cystinyl peptides produced by chemical and enzymatic digestions. A unique structure, named the apple domain, was established for each of the four tandem repeats in the amino-terminal portion of the molecule. The apple domains (90 or 91 amino acids) contain 3 highly conserved disulfide bonds linking the first and sixth, second and fifth, and third and fourth half-cystine residues present in each repeat. The fourth tandem repeat contains an extra disulfide bond that forms a second small loop within the apple domain. The carboxyl-terminal portion of plasma prekallikrein containing the catalytic region of the molecule was found to have disulfide bonds located in positions similar to those of other serine proteases.

引用

页码：2050 / 2056

页数：7

共 34 条

[1]

BAGLIA FA, 1990, J BIOL CHEM, V265, P4149

[2]

BOUMA BN, 1977, J BIOL CHEM, V252, P6432

[3] HUMAN-PLASMA PREKALLIKREIN, A ZYMOGEN TO A SERINE PROTEASE THAT CONTAINS 4 TANDEM REPEATS [J].