A study of the acid phosphatase of Treponema denticola.
This study describes some of the properties of the acid phosphatase of the potential periodontopathogen Treponema denticola. The highest enzyme activity was found in 87 h old cells. Two optimum pHs for enzyme activity were detected, one at pH 4.8 and another at pH 6.2. Divalent cations did not influence the acid phosphatase of T. denticola. The anion F- added in the form of NaF and at a level greater than 20 micrograms/ml F- diminished the activity of the acid phosphatase of intact cells of T. denticola. The addition of 10 micrograms/ml F- as SnF2 induced a statistically significant reduction of acid phosphatase activity. The apparent Km for the acid phosphatase was 7.3 mM with p-nitrophenyl phosphate as substrate. Fluoride appeared to be a noncompetitive inhibitor of the enzyme with an apparent Ki of 0.3 mM. Acid phosphatase may be released partially in osmotic shock fluids. Also, 7-diazonium-1, 3-naphthalene disulfonate, which is incapable of penetrating the bacterial permeability barrier and is known to inactivate enzymes found in the bacterial periplasmic place, suppressed the activity of the acid phosphatase in intact cells of T. denticola.
Norton Hughes
C A
CA
Department of Microbiology, Loyola University Stritch School of Medicine, Maywood, IL 60153.
Yotis
W W
WW
D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D005459:Fluorides / Q000494:pharmacology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D014208:Treponema / Q000201:enzymology*
D000135:Acid Phosphatase; D005459:Fluorides