TWO FORMS OF ADENOSINE DEAMINASE IN PIG EPIDERMIS

Abstract

ABSTRACT Molecular heterogeneity of adenosine deaminase in pig epidermis is reported. Gel filtration of pig skin extracts with Sephadex G‐150 revealed the existence of two forms of adenosine deaminase. Molecular weights of the enzymes were around 30,000–40,000 and 300,000–350,000 respectively. Several catalytic properties of these two adenosine deaminases were quite similar: Km value, substrate specificity, pH activity profile, and the effect of coformycin, a strong inhibitor of adenosine deaminase.