Characterization and novel activation of 72-kDa metalloproteinase in retinal interphotoreceptor matrix and Y-79 cell culture medium
BE Jones, P Moshyedi, S Gallo, J Tombran-Tink… - Experimental eye …, 1994 - Elsevier
Abstract Analysis of bovine interphotoreceptor matrix and conditioned medium from human
Y-79 retinoblastoma cells by gelatin SDS-PAGE zymography reveals abundant activity of a
72-kDa M r gelatinase. The 72-kDa gelatinase from either source is inhibited by EDTA but
not aprotinin or NEM, indicating that it is a metalloproteinase (MMP). The 72-kDa MMP is
converted to a 62-kDa species with APMA treatment after gelatin sepharose affinity
purification, typical of previously described gelatinase MMP-2. The latent 72-kDa gelatinase …
Y-79 retinoblastoma cells by gelatin SDS-PAGE zymography reveals abundant activity of a
72-kDa M r gelatinase. The 72-kDa gelatinase from either source is inhibited by EDTA but
not aprotinin or NEM, indicating that it is a metalloproteinase (MMP). The 72-kDa MMP is
converted to a 62-kDa species with APMA treatment after gelatin sepharose affinity
purification, typical of previously described gelatinase MMP-2. The latent 72-kDa gelatinase …