Purification and characterization of a phosphatase specifically hydrolyzing p-nitrophenyl phosphate from an oral strain of Streptococcus mutans

Arch Biochem Biophys. 1972 Oct;152(2):685-701. doi: 10.1016/0003-9861(72)90265-2.
No abstract available

MeSH terms

  • Amino Acids
  • Binding Sites
  • Cations, Divalent
  • Cellulose
  • Chromatography, DEAE-Cellulose
  • Chromatography, Gel
  • Cobalt
  • Edetic Acid
  • Enzyme Activation
  • Hydrogen-Ion Concentration
  • Isoelectric Focusing
  • Kinetics
  • Magnesium
  • Molecular Weight
  • Nitrophenols
  • Organophosphorus Compounds
  • Phosphoric Monoester Hydrolases* / antagonists & inhibitors
  • Phosphoric Monoester Hydrolases* / isolation & purification
  • Solubility
  • Streptococcus / enzymology*
  • Streptococcus / growth & development
  • Structure-Activity Relationship
  • Sulfhydryl Reagents
  • Vibration

Substances

  • Amino Acids
  • Cations, Divalent
  • Nitrophenols
  • Organophosphorus Compounds
  • Sulfhydryl Reagents
  • Cobalt
  • Cellulose
  • Edetic Acid
  • Phosphoric Monoester Hydrolases
  • Magnesium