ABSTRACT:
Alkaline phosphatase (orthophosphoric monoester phosphohydrolase EC 3.1.3.1.) was extracted from the small intestines of the rainbow lizard Agama agama, partially purified by DEAE-cellulose and Sephadex G-200 column chromatography and characterized.2.2. The enzyme had an optimum pH at 9.5 in sodium carbonate/bicarbonate buffer: a Km of 1.6 mM with p-nitrophenyl phosphate; a molecular weight of 132,000; was inhibited by Zn2+, EDTA, urea and phenylalanine; stimulated by Co2+, Mn2+ and Mg2+, but Ca2+ had little or no effect on the activity of the enzyme.3.3. The inhibition by urea was non-competitive, that by phenylalanine was uncompetitive. The enzyme was heat-labile.
Comparative biochemistry and physiology. B, Comparative biochemistry 01/1980; 67(1):41-47. DOI:10.1016/0305-0491(80)90266-7
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