Potassium glucose 6-O-sulphate as a substrate for glycosulphatase

Abstract

Solutions of hydrazine catalyze the partial desulphation of the disulphate esters of glucose and galactose. Quantitative results show that, under standard conditions (pH 5.3 in 0.5 M-sodium acetate-acetic acid buffer at 38[degree]), galactose disulphate is desulphated more rapidly than the corresponding glucose derivative and suggest that in each case one ester sulphate group only is readily removed. The 6-O-monosulphate esters of glucose and galactose and the 3-O-monosulphate of glucose are not readily desulphated by hydrazine. Unsuccessful attempts have been made to detect the presence in mammalian tissues of enzymes capable of liberating sulphate from monosaccharide sulphate esters, chondroitin sulphates A and C and from various sulphated oligosaccharides derived from chondroitin sulphate A.