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A 25 kDa α 2 ‐microglobulin‐related protein is a component of the 125 kDa form of human gelatinase
Author(s) -
Triebel Susanne,
Bläser Jörg,
Reinke Heinz,
Tschesche Harald
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81511-j
Subject(s) - gelatinase , biochemistry , chemistry , dimer , beta 2 microglobulin , monomer , sepharose , disulfide bond , peptide sequence , fibroblast activation protein, alpha , microbiology and biotechnology , enzyme , biology , gene , genetics , organic chemistry , cancer , immunology , polymer
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 23 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 α 2 ‐microglobulin‐related protein from rats, a protein so far unknown in humans.