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An Insulin Degrading Proteinase from Human Erythrocytes and Its Inhibition by Proteinase Inhibitors

  • H. Tschesche
  • T. Dietl
  • H. J. Kolb
  • E. Standl
Conference paper
Part of the Bayer-Symposium book series (BAYER-SYMP, volume 5)

Abstract

Hemolytical serum or crude homogenates of red blood cells have long been known to inactivate or degrade insulin [1–4]. When a possible effect of insulin on red cell metabolism was investigated, this very fact occurred to us as a troublesome problem [5]. The half-life of the turnover of the insulin molecule in the human system has been found to be about 12–40 min. The degradation of insulin has been attributed to two different pathways: a) reductive cleavage of the disulfide bridges by means of an enzyme (glutathione-insulin-transhydrogenase) [6–15], and b) proteolytic degradation by an insulin-specific proteinase [16–22].

Keywords

Trypsin Inhibitor Human Erythrocyte Helix Pomatia Bovine Colostrum Hemolyzed Erythrocyte 
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

© Springer-Verlag 1974

Authors and Affiliations

  • H. Tschesche
    • 1
  • T. Dietl
    • 1
  • H. J. Kolb
    • 2
  • E. Standl
    • 2
  1. 1.Lehrstuhl für Organische Chemie und BiochemieOrganisch-Chemisches Laboratorium der Technischen Universität MünchenMunichFed. Rep. Germany
  2. 2.Institut für DiabetesforschungMunichFed. Rep. Germany

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