Partial purification and biochemical properties of acid and alkaline phosphatases from Myxococcus coralloides D

F. GONZALEZ, M.E. FAREZ-VIDAL, J.M. ARIAS AND E. MONTOYA. 1994. Acid phosphatase and alkaline phosphatase from vegetative cells of Myxococcus coralloides D were purified by two chromatographic steps. The molecular weights were estimated by gel filtration and SDS-PAGE. Optimum 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 phosphatase, 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 Km values of the acid and alkaline phosphatases for p-nitrophenylphosphate were 5.0 times 10-3 mol ***l-1 and 1.5 times 10-3 mol l-1, respectively.