Purification and some properties of membrane-bound and soluble pyrophosphatases of yeast vacuoles. |
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Authors: | L Lichko L Okorokov |
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Affiliation: | Institute of Biochemistry and Physiology of Microorganisms, U.S.S.R. Academy of Sciences, Puschino, Moscow Region. |
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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. |
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Keywords: | Yeast vacuoles pyrophosphatase H+-transport |
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