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Purification and some properties of membrane-bound and soluble pyrophosphatases of yeast vacuoles
1Institute of Biochemistry and Physiology of Microorganisms, U.S.S.R. Academy of Sciences, Puschino, Moscow Region.
Yeast (Chichester, England)
|November 1, 1991
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.