ASSIGNMENT OF DISULFIDE BONDS IN THE X-PROTEIN (HBX) OF HEPATITIS-B VIRUS

被引：25

作者：

GUPTA, A ^{[1
]}

MAL, TK ^{[1
]}

JAYASURYAN, N ^{[1
]}

CHAUHAN, VS ^{[1
]}

机构：

[1] INT CTR GENET ENGN & BIOTECHNOL,NEW DELHI 110067,INDIA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 212卷 / 03期

关键词：

D O I：

10.1006/bbrc.1995.2057

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：

We have established the disulphide arrangement of cysteines in E. coli expressed HBx by chromatographic analysis of enzymatically cleaved protein and sequence analysis of cysteine containing fragments. Eight of the nine cysteines are disulphide linked in an interesting pattern. Each cysteine is linked to the fourth cysteine in a sequential manner and the last cysteine is free; the disulphide linkages are between Cys(7) and Cys(78), CyS(17) and CyS(115), Cys(61) and Cys(137), Cys(69) and CyS(143) while Cys(148) is free. (C) 1995 Academic Press, Inc.

引用

页码：919 / 924

页数：6

共 8 条

[1] A PROCEDURE FOR INSITU ALKYLATION OF CYSTINE RESIDUES ON GLASS-FIBER PRIOR TO PROTEIN MICROSEQUENCE ANALYSIS [J].