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Characterization of cell-bound papain-soluble beta-lactamases in BRO-1 and BRO-2 producing strains ofMoraxella (Branhamella) catarrhalis andMoraxella nonliquefaciens

  • I. Eliasson
  • C. Kamme
  • M. Vang
  • S. G. Waley
Article

Abstract

InMoraxella (Branhamella) catarrhalis andMoraxella nonliquefaciens strains isolated from clinical specimens in the south of Sweden two variants of beta-lactamase were distinguished by isoelectric focusing (IEF). The BRO-1 (Ravasio type) enzyme was the most common inBranhamella catarrhalis, constituting about 90% of the beta-lactamase found in this species, while the BRO-2 enzyme (1908 type) was as common as BRO-1 inMoraxella nonliquefaciens. The determinants mediating the production of BRO-1 and BRO-2 were both transferable by conjugation. Cell-bound beta-lactamase from reference strains producing BRO-1 and BRO-2 could be solubilized by papain digestion. The isoelectric point of the solubilized enzymes differed distinctly between BRO-1 (pI 6.5) and BRO-2 (pI 6.9). The molecular species of BRO-1 and BRO-2 released by papain digestion were purified by affinity chromatography with phenylboronic acid agarose gel. They had identical molecular weights of approximately 28,000. Their kinetic constants were indistinguishable for a number of substrates and beta-lactamase inhibitors.

Keywords

Molecular Weight Internal Medicine Agarose Isoelectric Point Affinity Chromatography 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Friedr. Vieweg & Sohn Verlagsgesellschaft mbH 1992

Authors and Affiliations

  • I. Eliasson
    • 1
  • C. Kamme
    • 1
  • M. Vang
    • 1
  • S. G. Waley
    • 2
  1. 1.Department of Medical MicrobiologyUniversity of LundLundSweden
  2. 2.Sir William Dunn School of PathologyUniversity of OxfordOxfordUK

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