Purification and some properties of membrane‐bound and soluble pyrophosphatases of yeast vacuoles

Abstract

The membrane-bound and soluble pyrophosphatase (PPase) activities of Saccharomyces carlsbergensis vacuoles are determined by the functioning of special enzymes and are not due to non-specific PPi hydrolysis by other vacuolar phosphohydrolases. The molecular mass of the membrane-bound PPase is apparently 120,000 and its molecule consists of three subunits with Mr = 41,000. Soluble PPase has a molecular mass of about 82,000 and includes three subunits with Mr = 28,000. Both enzymes are glycoproteins. The vacuolar membrane-bound PPase is a proton pump.