SOME SYNTHETIC AND HYDROLYTIC EXPERIMENTS WITH CHYMOTRYPSIN

Max Bergmann(Rockefeller Foundation), Joseph S. Fruton(Rockefeller Foundation)
Journal of Biological Chemistry
June 1, 1938
Cited by 113Open Access
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Abstract

The process of the gastrointestinal digestion of food proteins is generally assumed to involve only the breakdown of the proteins into amino acids.Thus peptic and tryptic proteinases are supposed to perform exclusively hydrolytic reactions under the physicochemical conditions prevalent during digestion.Recent experiments (1, 2) have shown that the intracellular proteinases papain, cathepsin, and bromelin are capable of synthesizing hippurylanilide from hippuric acid and aniline and also benzoyl-l-phenylalanyl-Lleucine anilide from benzoyl-l-phenylalanine and kleucine anilide.It has now been observed that a preparation of crystalline chymotrypsin effects the synthesis of benzoyl-Ltyrosylglycine anilide from benzoyl-Z-tyrosine and glytine anilide.


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