| Literature DB >> 5158391 |
Abstract
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.Entities:
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Year: 1971 PMID: 5158391 PMCID: PMC1331634 DOI: 10.1113/jphysiol.1971.sp009665
Source DB: PubMed Journal: J Physiol ISSN: 0022-3751 Impact factor: 5.182