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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.

DOI:10.1111/j.1574-6968.1993.tb06077.x
PMID:8472928
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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