Enzymatic sulfation of mucopolysaccharides in hen oviduct. I. Transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate to mucopolysaccharides.

The oviduct of the laying hen is an organ histologically differentiated into four areas, each with a unique function in the biosynthesis of the egg (2). It contains high concentrations of a number of unusual nucleotides, including uridine diphosphoacetylgalactosamine and uridine diphosphoacetylgalactosamine-(4?)sulfate (3). More recently, it has been observed that uridine diphosphoacetylgalactosamine sulfate, previously isolated from whole oviduct, is localized within a 2-cm segment of oviduct, termed the isthmus1 S35-inorganic sulfate given to hens is taken up by the oviduct only in the isthmus and in the vagina, the terminal 3-cm region of oviduct. Furthermore, the isthmus is concerned physiologically with the synthesis of the inner egg shell membranes. These membranes contain a sulfated mucopolysaccharide, the exact structure of which has not yet been estab1ished.l These observations have led to the present study of the biosynthesis of sulfated mucopolysaccharides in the isthmus of oviduct. The observations reported in the present papers are concerned with enzymatic mechanisms of mucopolysaccharide sulfation in the isthmus. In the first paper an enzymatic reaction will be described in which sulfate is transferred from phosphoadenosine 5’-phosphosulfate (“active sulfate” of Robbins and Lipmann (4)) to a number of mucopolysaccharide acceptors. Enzymes which catalyze the synthesis of phosphoadenosine 5’-phosphosulfate from inorganic sulfate have also been isolated from isthmus. Data presented in the following two papers (5, 6) have led to elucidation of the mechanism of the sulfation reaction. The transfer of sulfate to polysaccharides from phosphoadenosine 5’phosphosulfate by extracts of embryonic chick cartilage (7) and from p-nitrophenyl sulfate by extracts of the snail, Charonia Zampas, (8) have been previously investigated.