Partial purification and biochemical properties of acid and alkaline phosphatases from Myxococcus coralloides D |
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| Authors: | F González M Esther Fárez-Vidal JM Arias E Montoya |
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| Institution: | Departamento de Microbiologia, Facultad de Ciencias, Universidad de Granada, Granada, Spain |
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| 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 K m 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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