Purification and characterization of three carboxylesterases from Enterobacteriaceae

FEMS Microbiol Lett. 1993 Mar 15;108(1):81-5. doi: 10.1111/j.1574-6968.1993.tb06077.x.

Abstract

The carboxylesterases from Proteus vulgaris, Salmonella enterica and Citrobacter amalonaticus were purified 104-, 95- and 120-fold, respectively by chromatography. The enzymes had similar catalytic activities but differed considerably in their inactivation by heat, di-isopropyl fluorophosphate and Cd2+, Zn2+, Hg2+ and Cu2+. Quantitative neutralization of hydrolytic activity with specific immunoglobulins indicated that the three enzymes were antigenically distinct.

Publication types

  • Comparative Study

MeSH terms

  • Carboxylic Ester Hydrolases / antagonists & inhibitors
  • Carboxylic Ester Hydrolases / isolation & purification*
  • Carboxylic Ester Hydrolases / metabolism
  • Citrobacter / enzymology
  • Enterobacteriaceae / enzymology*
  • Hot Temperature
  • Immunochemistry
  • Isoelectric Point
  • Isoflurophate / pharmacology
  • Kinetics
  • Metals / pharmacology
  • Molecular Weight
  • Proteus vulgaris / enzymology
  • Salmonella / enzymology
  • Substrate Specificity

Substances

  • Metals
  • Isoflurophate
  • Carboxylic Ester Hydrolases