By R. Jahrreiss, E. Habermann (auth.), F. Sicuteri, M. Rocha e Silva, Nathan Back (eds.)
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Additional resources for Bradykinin and Related Kinins: Cardiovascular, Biochemical, and Neural Actions
Next, the preparation of human 'kininogenase II' used by Vogt and Wawretschek (1968) was examined. The preparation is obtained in the same way as 'B-depleted plasma' (Margolis, 1960): extensive treatment of plasma with glass is assumed to use up kininogenase I, leaving only pre-kininogenase II. The latter can be activated by renewed glass contact, and should act on rat, but not on dog kininogen. More activity was found adsorbed on to the activating glass powder, than in the supernatant plasma; the enzyme in both phases proved more effective on heated dog plasma than on heated rat plasma.
Werle, E. in "Polypeptides which affect smooth muscles and blood vessels", M. , p. 199. Pergamon Press, Oxford, 1960. Bar-Eli, A. and E. Katchalski. J. Biol. Chern. 238: 1690, 1963. 1: KININ FORMATION IN HUMAN BLOOD SERUM INDUCED BY COOLING AND BY HEAT AGGREGATED HUMAN GAMMA GLOBULIN PREPARATIONS Desiree Armstrong and W. Dias da Silva The Middlesex Hospital tv\edical School, London, England, and the Federal University of MinasGerais, Belo Horizonte, Brazil The original kinin research at the Middlesex Hospital Medical School concerned, for many years, the occurrence of plasma kinin when the human plasma touched foreign surface such as glass (Armstrong et ai, 1952, 1957; Keele & Armstrong, 1964; Armstrong, 1968a).
Peptide, and this structure was determined by a combination of carboxypeptidase and leucine aminopeptidase methods (KATO, SUZUKI, 1968). As given in Table III, from this BrCN peptide, trypsin, pancreatic kallikrein and snake venom enzyme liberated kallidin only hydrolyzing arginylseryl bond, although trypsin and venom enzyme liberate bradykinin from the intact kininogen. The reason why trypsin did not hydrolyze the lysylarginyl bond may be explainable from the fact that the amino group of N-terminal lysine is free in this peptide.