Studies in detoxication. 43. A study of the arylsulphatase activity of takadiastase towards some phenolic ethereal sulphates

Abstract

The arylsulfatase activity of tak-adiastase was tested on the salts of o-, m-, and p-nitro-, p-chloro, p-aldehydo, 4-hvdroxy-2-nitro-, 4-hydroxy-3-nitro and 2-hydroxy-5-nitro- phenylsulfuric acids by spectroscopic measurement of the liberated phenol. The pH optimum was 5.8-6.4 varying slightly with the substrate. Values were given for the optimal substrate concn. and Km. K-4-hydroxy-3-nitrophenylsulfate was not hydrolyzed by the enzyme and inhibited its action on other sulfates due to formation of a stable enzyme-substrate complex. KCN, K2SO3, Na2SO3 and hydroxylamine, agents reacting with aldehydes, were inhibitory but common inorganic ions were not.