Purification and some properties of membrane-bound and soluble pyrophosphatases of yeast vacuoles.
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.
Lichko
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L
Institute of Biochemistry and Physiology of Microorganisms, U.S.S.R. Academy of Sciences, Puschino, Moscow Region.
Okorokov
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D000251:Adenosine Triphosphatases / Q000378:metabolism; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000201:enzymology; D011755:Pyrophosphatases / Q000302:isolation & purification* / Q000378:metabolism; D012440:Saccharomyces / Q000201:enzymology* / Q000648:ultrastructure; D014617:Vacuoles / Q000201:enzymology*
D000251:Adenosine Triphosphatases; D011755:Pyrophosphatases