Abstract
F. GONZÁLEZ, M.E. FÁREZ‐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.
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