Electrophoretic charaterization of ATP-sulfate adenylyltransferase (ATP-sulfurylase) using acrylamide gels

Abstract A technique for the electrophoretic characterization of ATP: sulfate adenylyltransferase is described. Sites of enzymic activity in gels were recognized by detecting, in situ , the pyrophosphate that resulted from the molybdolysis of ATP. The method was successful for demonstrating, in gels, the activity of a partially purified but highly active ATP: sulfate adenylyltransferase from spinach. It was also used to detect the presence of the enzyme in soluble protein extracts of twelve selected strains of sulfate-reducing bacteria. Some possible applications of the method are discussed.