ABSTRACT:
DEAE-cellulose chromatography of mycelial alkaline phosphatase (orthophosphoric monoester phosphohydrolase, EC 3.1.3.1) from Basidiobolus haptosporosus, produced three iso-enzymes “A”, “B” and “C”.2.2. Fraction “A” was further characterized and showed maximum activity at pH 10 in 0.1 M sodium carbonate-bicarbonate buffer.3.3. The enzyme was stimulated by Mg2+, Co2+ and Mn2+ and inactivated by Zn2+, Cu2+, EDTA, citrate and tartrate.4.4. Phosphate ions inhibited it competitively, phenylalanine uncompetitively and urea noncompetitively.5.5. It was heat stable for 60 min at 37°C but labile above 55°C.6.6. Its Km with p-nitrophenylphosphate was 0.5 mM; its estimated molecular weight was 160,000.7.7. The results are compared with the properties of alkaline phosphatases from the rainbow lizard and man and discussed in terms of a triadic association between the fungus, the lizard and man.
Comparative biochemistry and physiology. B, Comparative biochemistry 01/1981; 70(2):359-366. DOI:10.1016/0305-0491(81)90058-4
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