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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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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