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Vasopeptides pp 91-102 | Cite as

Observations on the Chymotrypsin Peptide Releasing Activity on Plasmas

  • Alba A. C. Lavras
  • Mina Fichman
  • Elisa Hiraichi
  • Tomoyo Tobo
  • Marisa A. Boucault
  • Paulina Schmuziger
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 21)

Abstract

Previous report1 has shown the liberation of a pharmacologically active principle by the action of Padutin on the Bothrops jararaca plasma and has demonstrated its distinction from kinins. Afterwards, experiments were carried out to clarify whether such release is due to kallikrein or to another enzyme present in Padutin as an impurity. Taking in account the chymotrypsin destructive ability on the active released substancel, this enzyme was reconsidered as a possible Padutin active contaminant. This hypothesis was reinvestigated by some experiments herein presented. On the other hand, this paper presents the results obtained in the study of chymotrypsin action extended from Bothrops jararaca to mammal plasmas.

Keywords

Incubation Mixture Aorta Strip Fresh Plasma Chymotrypsin Action Pressor Peptide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1972

Authors and Affiliations

  • Alba A. C. Lavras
    • 1
  • Mina Fichman
    • 1
  • Elisa Hiraichi
    • 1
  • Tomoyo Tobo
    • 1
  • Marisa A. Boucault
    • 1
  • Paulina Schmuziger
    • 1
  1. 1.Servico de Farmacologia de Instituto ButantanSao PauloBrasil

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