Heterogeneity of the basic pancreatic inhibitor (Kunitz) in various bovine organs.
Four protein protease inhibitors (I, II, III, IV) having low molecular weights (10 600-6500) and basic isoelectric points were isolated by affinity chromatography from bovine spleen. Inhibitor IV was identified as the basic pancreatic trypsin inhibitor (Kunitz inhibitor); the presence and distribution of components I, II and III vary in the different bovine organs. Spleen inhibitors I, II, III and IV were purified by ion-exchange chromatography; they form 1:1 complexes with trypsin and inhibit enzymatic activity of trypsin, chymotrypsin and kallikrein. Inhibitors I, II and III contain carbohydrate moieties (7-4%) covalently bound to the polypeptide chain. Specific basic pancreatic trypsin inhibitor antiserum has shown the complete identity between inhibitor IV and the basic pancreatic trypsin inhibitor, while partial cross-reactivity between the basic pancreatic trypsin inhibitor and inhibitors I, II and III can be seen from a double immunodiffusion test.
D000818:Animals; D007611:Aprotinin / Q000032:analysis* / Q000302:isolation & purification; D002417:Cattle; D008099:Liver / Q000032:analysis; D008168:Lung / Q000032:analysis; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000032:analysis* / Q000302:isolation & purification; D012469:Salivary Glands / Q000032:analysis; D013154:Spleen / Q000032:analysis; D013950:Thymus Gland / Q000032:analysis; D013961:Thyroid Gland / Q000032:analysis
D011480:Protease Inhibitors; D007611:Aprotinin