| Literature DB >> 1281792 |
S Triebel1, J Bläser, H Reinke, H Tschesche.
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.Entities:
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Year: 1992 PMID: 1281792 DOI: 10.1016/0014-5793(92)81511-j
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124