A 25 KDA ALPHA-2-MICROGLOBULIN-RELATED PROTEIN IS A COMPONENT OF THE 125-KDA FORM OF HUMAN GELATINASE

被引：210

作者：

TRIEBEL, S ^{[1
]}

BLASER, J ^{[1
]}

REINKE, H ^{[1
]}

TSCHESCHE, H ^{[1
]}

机构：

[1] UNIV BIELEFELD, FAC MED, BIOCHEM ABT, POSTFACH 100131, W-4800 BIELEFELD 1, GERMANY

来源：

FEBS LETTERS | 1992年 / 314卷 / 03期

关键词：

GELATINASE; ALPHA-2-MICROGLOBULIN-RELATED PROTEIN; METALLOPROTEINASE; LIPOCALIN;

D O I：

10.1016/0014-5793(92)81511-J

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：

Besides the monomeric mammalian 95 kDa progelatinase, two additional forms, a disulfide-bridged 220 kDa dimer and a 125 kDa form were isolated from human PMN leukocytes. The 125 kDa progelatinase was identified as a covalently linked, disulfide-bridged hetrodimer formed of the monomer with a 25 kDa protein. This 25 kDa protein was isolated from gelatinase bound to the affinity support of gelatin-Sepharose and eluted by DTE-containing buffer. The amino acid sequence of tryptic peptides of this protein revealed homology with an alpha2-microglobulin-related protein from rats, a protein so far unknown in humans.

引用

页码：386 / 388

页数：3

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