PARTIAL-PURIFICATION AND BIOCHEMICAL-PROPERTIES OF ACID AND ALKALINE-PHOSPHATASES FROM MYXOCOCCUS-CORALLOIDES-D

Acid phosphatase and alkaline phosphatase from vegetative cells of Myx ococcus coralloides D were purified by two chromatographic steps. The molecular weights were estimated by gel filtration and SDS-PAGE. Optim um pH, stability, optimum temperature and thermal inactivation studies were made for both enzymes. EDTA and other chelating agents inhibited alkaline but not acid activity. Mg2+ activated the alkaline phosphata se, while the acid phosphatase was inhibited by fluoride. Both enzymes degraded a number of phosphomonoesters, but were unable to hydrolyse either polyphosphates or cAMP. The K-m, values of the acid and alkalin e phosphatases for p-nitrophenylphosphate were 5.0 x 10(-3) mol l(-1) and 1.5 x 10(-3) mol l(-1), respectively.