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Purification and characterization of three carboxylesterases from Enterobacteriaceae
P Goullet1, A Brisabois, B Picard
1Laboratoire de Microbiologie, Faculté de Médecine Xavier Bichat, Université Paris 7, France.
FEMS Microbiology Letters
|March 15, 1993
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.