A 25 kDa α2‐microglobulin‐related protein is a component of the 125 kDa form of human gelatinase

作者：Susanne Triebel, Jörg Bläser, Heinz Reinke, Harald Tschesche · 发表于：FEBS Letters · 年份：1992 · DOI：10.1016/0014-5793(92)81511-j · 被引用次数：230 · 研究领域：Protease and Inhibitor Mechanisms、Peptidase Inhibition and Analysis、Cell Adhesion Molecules Research

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.