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Alkaline Phosphatase Activity in a Strain of Bacterionema Matruchotii
Colin K. Franker
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 Km 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.
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Journal of Dental Research, Vol. 58, No. 7,
1705-1708 (1979)
DOI: 10.1177/00220345790580071001

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