| pubmed-article:1833192 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1833192 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:1833192 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1833192 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:1833192 | lifeskim:mentions | umls-concept:C0008550 | lld:lifeskim |
| pubmed-article:1833192 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:1833192 | lifeskim:mentions | umls-concept:C0207108 | lld:lifeskim |
| pubmed-article:1833192 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1833192 | pubmed:dateCreated | 1991-11-1 | lld:pubmed |
| pubmed-article:1833192 | pubmed:abstractText | The dacB gene of Escherichia coli, coding for penicillin-binding protein 4 (PBP4) was cloned under the control of the phage lambda pR promoter and cro gene translation signals. Depression of the phage lambda promoter for 2 h at 42 degrees C in E. coli led to the maximum over-production of PBP4 to 3.8% of the total soluble protein. Expression at 42 degrees C but not at 40 degrees C or 37 degrees C led to incomplete processing and aggregation of the preform of PBP4. Cibacron navyblue 2G-E was selected from a collection of triazine dyes as having a high affinity for PBP4. The immobilised dye was used in a two-step procedure to isolated 374 mg PBP4 from the soluble fraction of 125 g (wet mass) cells of the over-producing strain, with a recovery of 63.2% and a final purity of 99% as determined by active-site titration with radiolabelled penicillin. Saturation of PBP4 with various beta-lactam derivatives did not abolish binding to the dye material, nor was PBP4 eluted by addition of beta-lactams from the dye matrix. PBP4 behaved as a soluble protein throughout the purification, that was performed in the complete absence of detergents. Furthermore, in flotation experiments on sucrose density gradients and in Triton X-114 fractionation experiments, it showed the characteristics of a soluble protein. Cibacron navyblue 2G-E showed class specificity for all E. coli PBP except PBP3 and could be used for the isolation of these PBP from membrane extracts. | lld:pubmed |
| pubmed-article:1833192 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1833192 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1833192 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1833192 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1833192 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1833192 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:1833192 | pubmed:author | pubmed-author:KeckWW | lld:pubmed |
| pubmed-article:1833192 | pubmed:author | pubmed-author:MottlHH | lld:pubmed |
| pubmed-article:1833192 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1833192 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1833192 | pubmed:volume | 200 | lld:pubmed |
| pubmed-article:1833192 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1833192 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1833192 | pubmed:pagination | 767-73 | lld:pubmed |
| pubmed-article:1833192 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:1833192 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1833192 | pubmed:articleTitle | Purification of penicillin-binding protein 4 of Escherichia coli as a soluble protein by dye-affinity chromatography. | lld:pubmed |
| pubmed-article:1833192 | pubmed:affiliation | University of Groningen, Department of Biochemistry, The Netherlands. | lld:pubmed |
| pubmed-article:1833192 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1833192 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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