title: Purification and properties of a beta-lactamase produced by Branhamella catarrhalis.
abstract: A beta-lactamase from Branhamella catarrhalis was purified by column chromatography. The purified enzyme hydrolyzed penicillins, such as ampicillin, carbenicillin, and piperacillin, more rapidly than cephalosporins. Furthermore, the enzyme hydrolyzed cefotaxime and cefmenoxime. The molecular weight of the enzyme was 33,000. The pI was 5.4.
mesh_terms: D000900:Anti-Bacterial Agents / Q000378:metabolism; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology*; D007700:Kinetics; D013379:Substrate Specificity; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000302:isolation & purification* / Q000378:metabolism; D047090:beta-Lactams
chemical_list: D000900:Anti-Bacterial Agents; D065093:beta-Lactamase Inhibitors; D047090:beta-Lactams; D001618:beta-Lactamases