F. Gonzalez et al., PARTIAL-PURIFICATION AND BIOCHEMICAL-PROPERTIES OF ACID AND ALKALINE-PHOSPHATASES FROM MYXOCOCCUS-CORALLOIDES-D, Journal of Applied Bacteriology, 77(5), 1994, pp. 567-573
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.