AFFINE SORBENTS WITH TRIPEPTIDE MORPHOLID E LIGANDS FOR PROTEASE ISOLATION

New affine sorbents were synthesized involving tripeptide morpholides H-Ala-Ala-Leu-Mrp and H-D-Ala-Leu-Arg-Mrp as ligands that mimic substr ates of subtilisin-like proteases and kallikrein, respectively. These were used for the isolation and purification of several proteases: try psin, pepsin, alpha-chymotrypsin, thrombin, kallikrein, and termitase and were also efficient in the isolation of proteolytic enzymes from c omplex mixtures, such as the urine of children suffering from glomerul onephritis, hepatopancreas of Kamchatka crab, and dandelion roots. The ligands are competitive inhibitors of a number of proteases, and ther efore, they were supposed to interact with the substrate binding sites in these enzymes.