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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 126 (1980), S. 251-256 
    ISSN: 1432-072X
    Keywords: Rhizobium leguminosarum ; Alkaline phosphatase ; Phosphomonoesterase ; Mg2+, Zn2+-enzyme, K+ activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The alkaline phosphatase (EC 3.1.3.1.) from Rhizobium leguminosarum WU235 has been purified. The enzyme is a non-specific phosphomonoesterase, has a molecular weight of 78,500 and a sub-unit molecular weight of 39,400. Magnesium and zinc ions are implicated in the structure of the enzyme; atomic absorption analysis gave 1.9 g-atoms Mg2+ and 1.9–5.1 g-atoms Zn2+ per mole of enzyme. In addition high concentrations of Mg2+ markedly stimulate the enzyme. The phosphatase is inhibited by Li+ and Na+ and stimulated by K+, Rb+ and Cs+, which suggests that the enzyme is K+ activated.
    Type of Medium: Electronic Resource
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