SOME PROPERTIES OF AN ALKALINE PHOSPHATASE FROM RAT ADIPOSE TISSUE

Abstract
An alkaline phosphatase was partially purified from aqueous extracts of rat adipose tissue, and some characteristics of the enzyme delineated. Among salient features, the enzyme is strongly inhibited by cysteine and ethylene diaminetetraacetic acid (EDTA) and types of inhibition were determined. Cysteine induced "complete exclusive" inhibition, while EDTA caused "partial" inhibition. Kinetic data on the inhibition by EDTA are consistent with a mechanism which does not involve chelation of a metallic cation. Various other properties of the enzyme are discussed.