| pubmed-article:773294 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0030958 | lld:lifeskim |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0007732 | lld:lifeskim |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0030842 | lld:lifeskim |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0597979 | lld:lifeskim |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0199176 | lld:lifeskim |
| pubmed-article:773294 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:773294 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:773294 | pubmed:dateCreated | 1976-7-6 | lld:pubmed |
| pubmed-article:773294 | pubmed:abstractText | The degree of peptidoglycan cross-linking has been studied in growing cells of a Dap(-) Lys(-) auxotroph of Escherichia coli K-12 by following the incorporation of [(3)H]diaminopimelic acid into the lysozyme digestion products of crude, isolated peptidoglycan. The percentage of inhibition of cross-linking increases with increasing concentrations of penicillin G, cephaloridine, and cefuroxime. When the R factor R1drd 19 was introduced into the strain by conjugation, it was found that the type IIIa, beta-lactamase specified by the plasmid was able to protect the cross-linking target against inhibition by penicillin G but not against cephaloridine, even though the beta-lactamase hydrolyzes this substrate 50% faster than penicillin G. Cefuroxime, which is completely resistant to hydrolysis by the type IIIa beta-lactamase, inhibited the peptidoglycan cross-linking target in both the R(+) and R(-) variants of the assay strain. A mutant plasmid, R1drd19amp2, which specified no type IIIa beta-lactamase synthesis, could not provide protection of the cross-linking target against penicillin G. The significance of these results, in relation to the ability of the antibiotics to pass the permeability barrier of the bacterial envelope, is discussed. | lld:pubmed |
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| pubmed-article:773294 | pubmed:language | eng | lld:pubmed |
| pubmed-article:773294 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:773294 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:773294 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:773294 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:773294 | pubmed:issn | 0066-4804 | lld:pubmed |
| pubmed-article:773294 | pubmed:author | pubmed-author:HughesJ MJM | lld:pubmed |
| pubmed-article:773294 | pubmed:author | pubmed-author:CurtisN ANA | lld:pubmed |
| pubmed-article:773294 | pubmed:author | pubmed-author:RossG WGW | lld:pubmed |
| pubmed-article:773294 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:773294 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:773294 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:773294 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:773294 | pubmed:pagination | 208-13 | lld:pubmed |
| pubmed-article:773294 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:773294 | pubmed:year | 1976 | lld:pubmed |
| pubmed-article:773294 | pubmed:articleTitle | Inhibition of peptidoglycan cross-linking in growing cells of Escherichia coli by penicillins and cephalosporins, and its prevention by R factor-mediated beta-lactamase. | lld:pubmed |
| pubmed-article:773294 | pubmed:publicationType | Journal Article | lld:pubmed |
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