title: The interaction of anthraquinone dyes with the plasmid-mediated OXA-2 beta-lactamase.
abstract: Although beta-lactamases do not require any nucleotide co-substrates, the OXA-2 type is inhibited competitively by Cibacron Blue 3GA, and by other anthraquinone dyes, including some simpler compounds with no side chain. The enzyme causes a red shift in the spectrum of Cibacron Blue. The beta-lactamase can be adsorbed in Blue Sepharose and specifically eluted by benzylpenicillin. These results indicate that the binding of anthraquinone dyes is a specific effect similar to that seen with many nucleotide-binding enzymes.
mesh_terms: D000873:Anthracenes / Q000494:pharmacology; D000880:Anthraquinones / Q000494:pharmacology*; D002846:Chromatography, Affinity; D004396:Coloring Agents / Q000494:pharmacology*; D007700:Kinetics; D011815:R Factors; D013053:Spectrophotometry; D014227:Triazines; D065093:beta-Lactamase Inhibitors
chemical_list: D000873:Anthracenes; D000880:Anthraquinones; D004396:Coloring Agents; D014227:Triazines; D065093:beta-Lactamase Inhibitors; C012842:Cibacron Blue F 3GA