Purification and characterization of the major cationic kallikrein inhibitor in bovine pituitary gland.
The presence of two types of kallikrein inhibitor (cationic and anionic inhibitors) was demonstrated in bovine pituitary gland. These kallikrein inhibitors were separated from the homogenate of bovine posterior pituitary by successive CM-Sephadex chromatography. The major cationic inhibitor was further purified to homogeneity by affinity chromatography using porcine pancreatic beta-kallikrein immobilized on Sepharose 4B and gel filtration. The complete amino acid sequence of this inhibitor was first determined, and it was shown to be a peptide of 58 residues with a calculated molecular weight of 6,511. The Ki value against bovine pituitary kallikrein was 6 x 10(-9) M. The cationic inhibitor was found to be identical with basic pancreatic trypsin inhibitor.
D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D002417:Cattle; D010450:Endopeptidases / Q000187:drug effects; D007610:Kallikreins / Q000037:antagonists & inhibitors*; D008969:Molecular Sequence Data; D010904:Pituitary Gland, Posterior / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D014361:Trypsin Inhibitors / Q000737:chemistry / Q000302:isolation & purification
D014361:Trypsin Inhibitors; D007611:Aprotinin; D010450:Endopeptidases; D007610:Kallikreins