Modification of Trypsin Pancreatic Inhibitor by Polysaccharides for Prolongation of Therapeutic Effect

Abstract

A polyvalent inhibitor of proteinases from the bovine pancreas effectively blocks the action of kallikrein, chymotrypsin, plasmin, plasmin activator, blood coagulation factors, and tissue and leukocytic proteinases (1). Owing to its wide specificity, this pancreatic inhibitor has long been used in therapeutic practice (2, 3). The great variety of the modes of action of the pancreatic inhibitor on the organism is illustrated by the list of possible targets for its curative effect (Fig. 1). This inhibitor is used in treating diseases associated with activation of the kinin systems in the organism (5). Such diseases include acute pancreatitis, primary hyperfibrinolytic hemorrhage and coagulopathy, burns, nephrotic syndrome, and shock of different etiology (4,6). Pancreatic inhibitor is very effective in normalizing the indices of the kinin system when large doses of this expensive preparation are used with these diseases. Large doses are needed because the inhibitor does not persist in the blood flow. The half-life of pancreatic inhibitor is 7 to 10 min depending on the species of the animal and on the dose (4,7). Also, it is desirable to maintain a high concentration of pancreatic inhibitor in the blood to prolong the inhibition.