Purification and characterization of three carboxylesterases from Enterobacteriaceae.
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.
Goullet
P
P
Laboratoire de Microbiologie, Faculté de Médecine Xavier Bichat, Université Paris 7, France.
Brisabois
A
A
Picard
B
B
D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002954:Citrobacter / Q000201:enzymology; D004755:Enterobacteriaceae / Q000201:enzymology*; D006358:Hot Temperature; D007120:Immunochemistry; D007526:Isoelectric Point; D007531:Isoflurophate / Q000494:pharmacology; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D008970:Molecular Weight; D011514:Proteus vulgaris / Q000201:enzymology; D012475:Salmonella / Q000201:enzymology; D013379:Substrate Specificity
D008670:Metals; D007531:Isoflurophate; D002265:Carboxylic Ester Hydrolases