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Alkaline Phosphatase Activity in a Strain of Bacterionema Matruchotii

Oral Biology Section and Dental Research Institute, School of Dentistry, University of California, Los Angeles, California 90024

Marlon P. Mcgee

Oral Biology Section and Dental Research Institute, School of Dentistry, University of California, Los Angeles, California 90024

Thomas P. Rezzo

Oral Biology Section and Dental Research Institute, School of Dentistry, University of California, Los Angeles, California 90024

Protein from the soluble fraction of Bacterium matruchotii cells propagated in a medium containing no added inorganic phosphate was fractionated by gel permeation chromatography. The bulk of phosphatase activity assayed at pH 8.0 was found in fractions equivalent to a molecular weight of 6 x 105 daltons. Substrate saturation kinetics indicate at K_m of 0.75 mM for p-nitrophenylphosphate. Activity was stimulated more than twofold by Zn++ at 1 mM, but was significantly reduced by EDTA, Ca++ and inorganic phosphate. The enzyme(s) shows negligible activity at pH below 6.0 and has a narrow optimum between 7.5 and 8.5.

Journal of Dental Research, Vol. 58, No. 7, 1705-1708 (1979)
DOI: 10.1177/00220345790580071001


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