[Purification of proteinases on bacitracin-modified silochromes with differing concentration of ligands and fragment lengths]

Abstract

The binding of subtilisin, bovine pancreatic trypsin, and human blood thrombin to bacitracin-modified silochromes differing in the ligand concentrations and arm lengths were studied. The optimal conditions for trypsin isolation and purification were found. Methods for isolation and purification of subtilisin and thrombin were developed that provided the extents of enzyme purification of 20-80. The specific activities of thrombin trypsin, and subtilisin were 1200-2625 NIH units per mg protein and 7-18 and 19-34 units per mg protein, respectively. The possibility of isolation and purification of trypsin, thrombin, and subtilisin on bacitracin-modified silochromes was demonstrated. The sorbents studied were suggested for industrial application.