@article{oai:mdu.repo.nii.ac.jp:00000351,
 author = {FUJIMURA, SETSUO and TANIGUCHI, HIROO and KANAGAWA, NAOHIRO and NAKAMURA, TAKESHI},
 issue = {1},
 journal = {松本歯学},
 month = {Jun},
 note = {application/pdf, Acid and alkaline phosphatases from an oral strin of Bacteroides melaninogenicus were purified to homogeneity from cell extracts and their properties were compared. Molecular weights of acid and alkaline phosphatases were estimated to be 62,000 and 160,000, respectively. Michaelis constant for p-nitrophenylphosphate of the acid phosphatase was 0.17 mM and that of the alkaline enzyme was 0.23 mM. The alkaline phosphatase was more stable than the acid phospatase when they were heated at 60℃. The activity of the acid phosphatase was largely reduced by Cu^<2+> or fluoride and the alkaline phosphatase was quite sensitive to inhibition by Zn^<2+>, thiol compounds, or EDTA. The inactivation by EDTA of the alkaline phosphatase was restored with Ca^<2+> or Mg^<2+>. The acid phosphatase hydrolyzed α-D-glucose 1.6-diphosphate, p-nitrophenylphos-phate, D-glucose 6-phosphate, and D-fructose 6-phosphate. On the other hand, p-nitro-phenylphosphate was the most suitable substrate for the alkaline phosphatase. Nucleoside triphosphates were also hydrolyzed by the alkaline phosphatase.},
 pages = {18--27},
 title = {Comparative Studies of Acid and Alkaline Phosphatases from Bacteroides melaninogenicus},
 volume = {9},
 year = {1983}
}