Comparison of the Kininogenase Activity of Human Pancreatic Trypsins and Porcine Kallikrein on Met-Lys-Bradykinin and Human Plasma Kininogen
- 1 January 1978
- journal article
- research article
- Published by Walter de Gruyter GmbH in Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie
- Vol. 359 (2) , 1225-1228
- https://doi.org/10.1515/bchm2.1978.359.2.1225
Abstract
Human trypsins 1 and 2 [EC 3.4.21.4] both converted Met-Lys-bradykinin to bradykinin and released bradykinin from kininogen in human plasma as measured by bioassay with the isolated guinea pig ileum. Porcine kallikrein [EC 3.4.21.8] did not act on Met-Lys-bradykinin and released kallidin from human kininogen. Since human trypsin 1 is only partially and trypsin 2 completely inhibited by soybean trypsin inhibitor, the criterion of susceptibility to soybean trypsin inhibitor cannot be used to discriminate between trypsin and kallikrein of different species.This publication has 5 references indexed in Scilit:
- Human pancreatic proteins: Amylase, proelastase, and trypsinogenArchives of Biochemistry and Biophysics, 1970
- Über das Sekretionsverhalten der spezifischen Trypsininhibitören und des Kallikreinogens beim Pankreas von Hund und MenschHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1967
- FURTHER STUDIES OF THE SENSITIZATION OF SMOOTH MUSCLE TO THE ACTION OF PLASMA KININS BY PROTEOLYTIC ENZYMESBritish Journal of Pharmacology and Chemotherapy, 1965
- THE NATURE OF THE KALLIDINS RELEASED FROM HUMAN PLASMA BY KALLIKREINS AND OTHER ENZYMESAnnals of the New York Academy of Sciences, 1963
- PURIFICATION AND SOME PROPERTIES OF THREE RALLIKREINSAnnals of the New York Academy of Sciences, 1963