PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED,ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES : III. KINETICS OF THE HEAT INACTIVATION OF PAPAIN,BROMELIN, AND ASCLEPAIN |
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| Authors: | Theodore Winnick Alva R. Davis David M. Greenberg |
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| Affiliation: | From the Departments of Botany and Biochemistry of the University of California, Berkeley |
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| Abstract: | 1. The rates of heat inactivation of papain, bromelin, and asclepain were determined at several different temperatures. Papain was by far the most resistant to heat. 2. The destruction of papain at 75–83° and bromelin at 55–70° followed the course of a first order reaction, except that for longer times of heating, bromelin (at 60–70°) was inactivated more rapidly than the first order equation required. 3. The rate of inactivation of asclepain at 55–70° followed the second order equation. 4. The critical thermal increments of inactivation of papain and bromelin, calculated with the van''t Hoff-Arrhenius equation, were of the same high order that has been found for protein denaturation. The increment for asclepain was somewhat lower. |
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