DISULFIDE BOND ASSIGNMENT IN HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES (TIMP)

被引：172

作者：

WILLIAMSON, RA

MARSTON, FAO

ANGAL, S

KOKLITIS, P

PANICO, M

MORRIS, HR

CARNE, AF

SMITH, BJ

HARRIS, TJR

FREEDMAN, RB

机构：

[1] CELLTECH LTD,SLOUGH SL1 4DY,BERKS,ENGLAND

[2] UNIV LONDON IMPERIAL COLL SCI & TECHNOL,DEPT BIOCHEM,LONDON SW7 2AZ,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1990年 / 268卷 / 02期

关键词：

D O I：

10.1042/bj2680267

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：

Disulphide bonds in human recombinant tissue inhibitor of metalloproteinases (TIMP) were assigned by resolving proteolytic digests of TIMP on reverse-phase h.p.l.c. and sequencing those peaks judged to contain disulphide bonds by virtue of a change in retention time on reduction. This procedure allowed the direct assignment of Cys-145-Cys-166 and the isolation of two other peptides containing two disulphide bonds each. Further peptide cleavage in conjunction with fast-atom-bombardment m.s. analysis permitted the assignments Cys-1-Cys-70, Cys-3-Cys-99, Cys-13-Cys-124 and Cys-127-Cys-174 from these peptides. The sixth bond Cys-132-Cys-137 was assigned by inference, as the native protein has no detectable free thiol groups.

引用

页码：267 / 274

页数：8