title: Induction of beta-lactamase from Shigella flexneri UCSF-129: purification by affinity chromatography and some properties.
abstract: Lincomycin, an inhibitor of protein synthesis, was an excellent inductor of beta-lactamase, and its total activity and specific activity were increased 2.5- and 3.6-fold respectively. The beta-lactamase produced by Shigella flexneri UCSF-129 was purified by affinity chromatography on phenylboronic acid-agarose with a type B column using an hydrophobic spacer arm (6-aminohexanoic acid activated with succinimide). The yield and specific activity were 96% and 29,283 U/mg, respectively. These were 1.7- and 3.8-fold higher, respectively, than those obtained by the traditional method using ion-exchange chromatography and gel filtration. The working-time was reduced to a third, and the enzyme preparation was shown to be pure by several criteria. From nine divalent cations assayed, only Sn(II) inhibited the enzyme by 74%, and the chloride ion did not have any effect on enzyme activity.
authors.affiliation: Department of Chemistry, Faculty of Science, University of Concepción, Chile.
authors.forename: M
authors.initials: M
authors.lastname: Campos
authors.forename: H
authors.initials: H
authors.lastname: González
authors.forename: M A
authors.initials: MA
authors.lastname: Alarcón
authors.forename: R
authors.initials: R
authors.lastname: Sánchez
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D002846:Chromatography, Affinity; D004790:Enzyme Induction / Q000187:drug effects; D008034:Lincomycin / Q000494:pharmacology; D012763:Shigella flexneri / Q000187:drug effects / Q000201:enzymology*; D001618:beta-Lactamases / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism
chemical_list: D000900:Anti-Bacterial Agents; D008034:Lincomycin; D001618:beta-Lactamases