Literature DB >> 1664997

Purification and some properties of membrane-bound and soluble pyrophosphatases of yeast vacuoles.

L Lichko1, L Okorokov.   

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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Year:  1991        PMID: 1664997     DOI: 10.1002/yea.320070805

Source DB:  PubMed          Journal:  Yeast        ISSN: 0749-503X            Impact factor:   3.239


  3 in total

1.  Characterization of a vacuolar pyrophosphatase in Trypanosoma brucei and its localization to acidocalcisomes.

Authors:  C O Rodrigues; D A Scott; R Docampo
Journal:  Mol Cell Biol       Date:  1999-11       Impact factor: 4.272

2.  Arbuscular mycorrhizal fungi induce differential activation of the plasma membrane and vacuolar H+ pumps in maize roots.

Authors:  Alessandro C Ramos; Marco A Martins; Anna L Okorokova-Façanha; Fábio Lopes Olivares; Lev A Okorokov; Nuno Sepúlveda; José A Feijó; Arnoldo R Façanha
Journal:  Mycorrhiza       Date:  2008-10-08       Impact factor: 3.387

3.  Molecular cloning and characterization of a soluble inorganic pyrophosphatase in potato.

Authors:  P du Jardin; J Rojas-Beltran; C Gebhardt; R Brasseur
Journal:  Plant Physiol       Date:  1995-11       Impact factor: 8.340

  3 in total

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