PMID: 7090Jan 1, 1976

Alkaline phosphatase of Thiobacillus thioparus. Partial purification and properties of the enzyme

Acta biochimica Polonica
M Galka, W Ostrowski


Soluble alkaline phosphatase from Thiobacillus thioparus cells was purified about 230-fold. The enzyme had a mol. wt. of 50 000 daltons, optimum pH at 10.5, and was heat-resistant in the presence of diethanolamine. Polyacrylamide-gel electrophoresis demonstrated contamination of the preparation with inactive proteins and the presence of two active bands. The enzyme activity was distinctly stimulated by increasing concentrations of Tris or diethanolamine. In the presence of glycine, 1 mM-Zn2+ enhanced the enzyme activity; in Tris or diethanolamine buffers the activity was stimulated by 1 mM-Mg2+ whereas Zn2+ had a strong inhibitory effect. Glycine at concentrations exceeding 25 mM also inhibited the enzyme. Specificity of the enzyme is fairly broad.

Related Concepts

Alkaline Phosphatase
Cations, Divalent
Cell Division Phases
Drug Stability
Enzyme Activation
Hydrogen-Ion Concentration
Structure-Activity Relationship
Thiobacillus thioparus

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