作者: M.P Sangorrı́n , E.J Folco , C.M Martone , J.J Sánchez
DOI: 10.1016/S1357-2725(01)00054-1
关键词: Serine Proteinase Inhibitors 、 Trypsin inhibitor 、 Kunitz STI protease inhibitor 、 Proteases 、 Trypsin 、 Serine protease 、 Proteinase 3 、 Protease 、 Molecular biology 、 Biochemistry 、 Biology
摘要: A trypsin proteinase inhibitor has been purified to homogeneity from the skeletal muscle of white croaker (Micropogon opercularis). Previously, we had described occurrence in fish a serine protease (proteinase I) which showed great capacity degrade whole myofibrils vitro and an endogenous that prevented action protease, both on natural artificial substrates. In this paper, report purification further biochemical characterization inhibitor. The was carried out by DEAE-Sephacel, Con A-Sepharose, Sephacryl S-300 Mono Q. Throughout procedure, inhibitory activity assayed using azocasein as substrate. molecular mass 65 kDa, estimated SDS-PAGE gel filtration. is glycoprotein, deduced fact it binds A-Sepharose stains with PAS wide range pH stability (from 5 11). thermal considerably decreased at temperatures >60 degrees C. Assays against various proteases indicated highly specific for proteases, since did not inhibit belonging any other groups. able target enzyme dose-dependent manner, 50% inhibition molar ratio close 1. present work contributes improving our understanding physiological role I-inhibitor system protein breakdown, well its influence post mortem proteolysis.