| pubmed-article:3493768 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3493768 | lifeskim:mentions | umls-concept:C0441833 | lld:lifeskim |
| pubmed-article:3493768 | lifeskim:mentions | umls-concept:C0597979 | lld:lifeskim |
| pubmed-article:3493768 | lifeskim:mentions | umls-concept:C0596260 | lld:lifeskim |
| pubmed-article:3493768 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:3493768 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:3493768 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3493768 | pubmed:dateCreated | 1987-3-30 | lld:pubmed |
| pubmed-article:3493768 | pubmed:abstractText | Beta-lactamases are divided into classes A, B and C on the basis of their amino acid sequences. Beta-Lactamases were incubated at pH 4.0 with the carboxy-group reagent 1-(3-dimethylaminopropyl)-3-ethylcarbodi-imide plus a coloured nucleophile and the extents of inactivation and nucleophile incorporation were monitored. Two class A enzymes (from Bacillus cereus and Bacillus licheniformis) and two class C enzymes (from Enterobacter cloacae P99 and Pseudomonas aeruginosa) were examined. All four enzymes were inactivated, with total inactivation corresponding to the incorporation of approx. 2-3 mol of nucleophile/mol of enzyme. In the case of beta-lactamase I from Bacillus cereus, some 53% of the incorporated nucleophile was located on glutamic acid-168 in the amino acid sequence. | lld:pubmed |
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| pubmed-article:3493768 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3493768 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3493768 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3493768 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3493768 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3493768 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3493768 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3493768 | pubmed:author | pubmed-author:WaleyS GSG | lld:pubmed |
| pubmed-article:3493768 | pubmed:author | pubmed-author:LittleCC | lld:pubmed |
| pubmed-article:3493768 | pubmed:author | pubmed-author:GagnonJJ | lld:pubmed |
| pubmed-article:3493768 | pubmed:author | pubmed-author:EmanuelE LEL | lld:pubmed |
| pubmed-article:3493768 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3493768 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3493768 | pubmed:volume | 240 | lld:pubmed |
| pubmed-article:3493768 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3493768 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3493768 | pubmed:pagination | 215-9 | lld:pubmed |
| pubmed-article:3493768 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:3493768 | pubmed:meshHeading | pubmed-meshheading:3493768-... | lld:pubmed |
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| pubmed-article:3493768 | pubmed:meshHeading | pubmed-meshheading:3493768-... | lld:pubmed |
| pubmed-article:3493768 | pubmed:meshHeading | pubmed-meshheading:3493768-... | lld:pubmed |
| pubmed-article:3493768 | pubmed:meshHeading | pubmed-meshheading:3493768-... | lld:pubmed |
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| pubmed-article:3493768 | pubmed:meshHeading | pubmed-meshheading:3493768-... | lld:pubmed |
| pubmed-article:3493768 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3493768 | pubmed:articleTitle | Carboxy groups as essential residues in beta-lactamases. | lld:pubmed |
| pubmed-article:3493768 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3493768 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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