| Autor: |
Triebel, Susanne, Bläser, Jörg, Reinke, Heinz, Tschesche, Harald |
| Zdroj: |
FEBS Letters; January 1992, Vol. 314 Issue: 3 p386-388, 3p |
| Abstrakt: |
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. |
| Databáze: |
Supplemental Index |
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