Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
294
pubmed:dateCreated
1993-3-30
pubmed:abstractText
The role of a residue of arginine at the active site of beta-lactamase from Shigella flexneri UCSF-129 was studied. It is a local pathogenic strain which produces intestinal problems, especially in children. Purified enzymes were obtained by affinity chromatography on phenylboronic acid-agarose gels. The enzyme was serine dependent with a molecular weight of 23.6 kD. It was specifically modified with phenylglyoxal (1/830 molar ratio) and incubated for 20 min in the presence of 50 mM sodium phosphate buffer at pH 8.3. The chemical change was established by isoelectric focusing, since a loss of one positive charge was detected. Protection by cephradine, a substrate, indicated the presence of a residue of arginine at its active site. Controls were conducted by differential spectroscopy. Similar results were obtained with 2,3,butanedione. This vital arginine stabilizes the negative charge of the carboxylic group of C-3 or C-4 from the substrates.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0026-2633
pubmed:author
pubmed:issnType
Print
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37-43
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
An arginine residue at the active site of beta-lactamase from Shigella flexneri UCSF-129.
pubmed:affiliation
Department of Chemistry, Faculty of Sciences, University of Concepción, Chile.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't