Kininogenase of the guinea-pig's coagulating gland and the release of bradykinin.
A kininogenase (CGK) in the coagulating gland of the guinea-pig was partially purified, characterized and separated from a kininase also present in the gland. This kininogenase is not inhibited by the usual kininogenase and protease inhibitors. Our results indicate that it is identical with the esterolytic enzyme in the gland which hydrolyses the synthetic ester TAME. The kinin released by CGK from dog's crude pseudoglobulin was purified more than 1500 times and identified as bradykinin by chromatography on paper, on carboxymethyl-cellulose columns, and on silica gel.
D000818:Animals; D001120:Arginine; D001920:Bradykinin; D002845:Chromatography; D002850:Chromatography, Gel; D002854:Chromatography, Paper; D002855:Chromatography, Thin Layer; D010450:Endopeptidases / Q000302:isolation & purification*; D004952:Esters; D005837:Genitalia, Male / Q000201:enzymology*; D006168:Guinea Pigs; D008297:Male; D008747:Methylcellulose; D011480:Protease Inhibitors; D012712:Serum Globulins; D014105:Tosyl Compounds
D004952:Esters; D011480:Protease Inhibitors; D012712:Serum Globulins; D014105:Tosyl Compounds; D008747:Methylcellulose; D001120:Arginine; D010450:Endopeptidases; D001920:Bradykinin