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Pepsin Inhibitory Activity amongst Activation Peptides of Pepsinogen

Nature volume 243, pages 417–419 (1973)Cite this article

Abstract

THE concept of the pepsin inhibitor (PI) and a method for its isolation in crystalline form from the acid-activated pepsinogen (Pg) system, in which pepsin (P) and other peptides (pp) are released (Pg→P+PI+pp), were advanced by Herriott1. PI was believed to interact with pepsin at pH 5 to 6, this inhibitory interaction being most readily observable in this pH range in the milk clotting system in which pepsin is believed to catalyse the reaction K-casein→para K casein+caseinomacropeptide.

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Authors and Affiliations

  1. Department of Pharmaceutical Technology, Royal College Building, University of Strathclyde, Glasgow, G1 1XW

    W. ANDERSON & J. E. HARTHILL

Authors
  1. W. ANDERSON
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  2. J. E. HARTHILL
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ANDERSON, W., HARTHILL, J. Pepsin Inhibitory Activity amongst Activation Peptides of Pepsinogen. Nature 243, 417–419 (1973). https://doi.org/10.1038/243417b0

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  • DOI: https://doi.org/10.1038/243417b0

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