Matrix metalloproteinase-1 in camel liver tissues: isolation, purification and some characterization

ABSTRACT

Matrix metalloproteinases [MMPs] constitute a multigene family of over 25 secreted and cell surface enzymes that process or degrade numerous pericellular substrates. Their targets include other proteinases, clotting factors, cell surface receptors, and virtually all structural extracellular matrix proteins The MMPs play a vital role in cellular functions as cell proliferation, tissue development, wound healing and tissue repair. In this study, a trial was carried out to isolate matrix metalloproteinase-l [MMP-1 collagenase, EC 3.4.24.7] from camel liver tissues [CaInelus dromedarius] in a small scale purification technique using ammonium sulphate fractionation, gel filtration on Sephadex G-100 and Bio-Gel A-1.5m column chromatographies. The homogeneity of the purified preparation was judged by polyacrylamide gel electrophoresis [PAGE] in the presence and absence of SDS and beta-mercaptoethanol. The enzyme is heterodimer and the molecular weight [M[r]] of the two subunits are 67 and 30 kDa, while that of the native enzyme is 97 kDa. The optimum temperature was in the range of 30-40°C EDTA was more potent inhibitor than DTT for enzyme activity