Purification and characterization of three carboxylesterases from Enterobacteriaceae.
作者信息
Goullet P, Brisabois A, Picard B
机构信息
Laboratoire de Microbiologie, Faculté de Médecine Xavier Bichat, Université Paris 7, France.
出版信息
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.
摘要
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