Affinity chromatography of proteases of hydroxyalkyl methacrylate gels with covalently attached inhibitors.

The efficient isolation of trypsin and chymotrypsin from a crude pancreatic extract was achieved by affinity chromatography on specific adsorbents prepared by coupling of both naturally occurring protease inhibitors and also synthetic low-molecular-weight protease inhibitors to hydroxyalkyl methacrylate gels. Specific sorbents prepared with synthetic inhibitors are stable and are suitable for the isolation of chymotrypsin and trypsin even on a large scale.