The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
STUDIES ON PROTEASE
I. The cleavability of various proteins by trypsin and papain
KOICHI NAKAMURA
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1940 Volume 31 Issue 2 Pages 311-322

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Abstract
The relative rates of hydrolysis of various animal and vegetable proteins by trypsin and papain were studied in relation to the initial reaction rates and to the optimum pH of proteolysis.
1. It was found that the relative ease with which proteins are hydrolyzed by trypsin diminishes in the following order.
Protamin>casein, edestin>vitellin, globin>gelatin, gliadin>serum globulin>serum albumin, legumin, egg albumin, ricin.
The optimum pH for hydrolysis lies between 8.7-9.0.
2. Papain hydrolyzes gelatin more readily than serum albumin, serum globulin and egg albumin. The comparative determination of the hydrolysis rates of other proteins could not be performed, as the majority of proteins examined separated out from the reaction fluids at a pH range of 4.0-6.0.
The author wishes to express his thanks to Assistant Prof. T. Uchino for his kind direction throughout this work.
Thanks are also due to the Royal. Academy. Fund for grants in aid of this investigation.
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© The Japanese Biochemical Society
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