title: [Purification and properties of intercellular inorganic pyrophosphatase from Saccharomyces cerevisiae].
abstract: An inorganic pyrophosphatase (EC3.6.1.1) from Saccharomyces cerevisiae was purified to PAGE homogeneity by sonication disruption, (NH4)2SO4 fractionation and DEAE-cellulose column chromatography. The optimum pH and temperature of the enzyme were 7.4-7.8 and 60 degrees C, respectively. The Km was 19.3 mmol/L. The enzyme required Mg2+ as a cofactor for hydrolysis of pyrophosphate and was inhibited by Ca2+, Hg2+, Pb2+, Mn2+.
authors.affiliation: Institute of Mirobiology, Chinese Academy of Sciences, Beijing 100080.
authors.forename: P
authors.initials: P
authors.lastname: Gou
authors.forename: S
authors.initials: S
authors.lastname: Yang
mesh_terms: D002848:Chromatography, DEAE-Cellulose; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D011755:Pyrophosphatases / Q000302:isolation & purification* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013696:Temperature
chemical_list: D011755:Pyrophosphatases