The effect of cations on the thermophilic character of alkaline phosphatase from Thermoactinomyces vulgaris.
The effect of cations on the thermophilic character of alkaline phosphatase from Thermoactinomyces vulgaris, is described. The optimal pH and temperature were 9.5 and 55 degrees C to 65 degrees C, respectively. The partial removal of cations with ethylene diamine tetraacetic acid converted the enzyme to mesophilic and susceptible to chemical denaturation. Their complete removal caused complete inhibition. The addition of 0.3mM cobalt and 10mM magnesium added before heating were found to be optimal for restoring its thermophilic character and its stability to a chemical denaturant.
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Dept. of Life Sciences, Bar-Ilan University, Ramat-Gan, Israel.
Pinsky
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Malovani
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D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D002413:Cations, Divalent / Q000494:pharmacology*; D002846:Chromatography, Affinity; D004492:Edetic Acid / Q000494:pharmacology; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008848:Micromonosporaceae / Q000187:drug effects / Q000201:enzymology*; D013696:Temperature
D002413:Cations, Divalent; D006146:Guanidines; D004492:Edetic Acid; D000469:Alkaline Phosphatase; D019791:Guanidine