PHYSICOCHEMICAL PROPERTIES OF THE PROTEOLYTIC ENZYME FROM THE LATEX OF THE MILKWEED, ASCLEPIAS SPECIOSA TORR. SOME COMPARISONS WITH OTHER PROTEASES

Author:

Winnick Theodore1,Davis Alva R.1,Greenberg David M.1

Affiliation:

1. From the Departments of Botany and Biochemistry of the University of California, Berkeley

Abstract

1. The kinetics of milk clotting by asclepain, the protease of Asclepias speciosa, were investigated. At higher concentrations of enzyme, the clotting time was inversely proportional to the enzyme concentration. 2. The digestion of casein and hemoglobin in 6.6 M urea by asclepain follows the second order reaction rate. The rate was roughly second order for casein in water. 3. Evaluation of the nature of the enzyme-substrate intermediate indicates that one molecule of asclepain combines with one molecule of casein or hemoglobin in urea solution. 4. Inhibition by the reaction products was deduced from the fact that the digestion velocity of hemoglobin in urea solution varied with the asclepain concentration in agreement with the Schütz-Borissov rule.

Publisher

Rockefeller University Press

Subject

Physiology

Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Kinetics of Biological Reactions with Special Reference to Enzymic Processes;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

2. Studies on Species of Asclepias. V. Chemistry †;Journal of the American Pharmaceutical Association (Scientific ed.);1952-06

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