PubMed:6332621 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/6332621","sourcedb":"PubMed","sourceid":"6332621","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/6332621","text":"Purification of beta-lactamases by affinity chromatography on phenylboronic acid-agarose.\nSeveral beta-lactamases, enzymes that play an important part in antibiotic resistance, have been purified by affinity chromatography on boronic acid gels. The procedure is rapid, appears to be selective for beta-lactamases, and allows a one-step purification of large amounts of enzyme from crude cell extracts. We have found the method useful for any beta-lactamase that is inhibited by boronic acids. Two kinds of boronic acid column have been prepared, the more hydrophobic one being reserved for those beta-lactamases that bind boronic acids relatively weakly. beta-Lactamase I from Bacillus cereus, P99 beta-lactamase and K 1 beta-lactamase from Gram-negative bacteria are among the better-known beta-lactamases that have been purified by this method. The procedure has also been used to purify a novel beta-lactamase from Pseudomonas maltophilia in high yield; the enzyme has an exceptionally broad substrate profile and hydrolyses monocyclic beta-lactams such as azthreonam and desthiobenzylpenicillin.","tracks":[]}