A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase

S Triebel; J Bläser; H Reinke; H Tschesche

doi:10.1016/0014-5793(92)81511-j

A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase

FEBS Lett. 1992 Dec 21;314(3):386-8. doi: 10.1016/0014-5793(92)81511-j.

Authors

S Triebel¹, J Bläser, H Reinke, H Tschesche

Affiliation

¹ Department of Biochemistry, Faculty of Chemistry, University of Bielefeld, Germany.

PMID: 1281792
DOI: 10.1016/0014-5793(92)81511-j

Abstract

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 heterodimer 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 alpha 2-microglobulin-related protein from rats, a protein so far unknown in humans.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Alpha-Globulins / analysis*
Amino Acid Sequence
Animals
Collagenases / chemistry*
Electrophoresis, Polyacrylamide Gel
Female
Humans
Male
Matrix Metalloproteinase 9
Molecular Sequence Data
Rats
Sequence Homology, Amino Acid

Substances

Alpha-Globulins
alpha(2)-microglobulin
Collagenases
Matrix Metalloproteinase 9