Literature DB >> 1096966

[Purification of beta-lactamases by affinity chromatography].

F Le Goffic, J Andrillon-Spiegel, R Letarte.   

Abstract

Affinity columns able to purifie beta-lactamases have been prepared either by linking covalently reversible inhibitors or substrates to agarose beds. The enzyme is eluted with a gradient of sodium chloride or released with the substrate. This method is a pertinent one for the purification of these enzymes and for the study of bacteria harbouring more than one beta-lactamase.

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Year:  1975        PMID: 1096966     DOI: 10.1016/s0300-9084(75)80106-4

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  3 in total

1.  Enzymatic and immunological characterization of a new cephalosporinase from Enterobacter aerogenes.

Authors:  R Letarte; M Devaud-Felix; J C Pechere; D Allard-Leprohon
Journal:  Antimicrob Agents Chemother       Date:  1977-08       Impact factor: 5.191

2.  The exocellular beta-lactamase of Streptomyces albus G. Purification, properties and comparison with the exocellular DD-carboxypeptidase.

Authors:  C Duez; J M Frère; D Klein; M Noël; J M Ghuysen; L Delcambe; L Dierickx
Journal:  Biochem J       Date:  1981-01-01       Impact factor: 3.857

3.  Characterization of three different beta-lactamases from the Bacteroides fragilis group.

Authors:  B Olsson-Liljequist; K Dornbusch; C E Nord
Journal:  Antimicrob Agents Chemother       Date:  1980-08       Impact factor: 5.191

  3 in total

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