| pubmed-article:11112509 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11112509 | lifeskim:mentions | umls-concept:C0014279 | lld:lifeskim |
| pubmed-article:11112509 | lifeskim:mentions | umls-concept:C2004454 | lld:lifeskim |
| pubmed-article:11112509 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:11112509 | lifeskim:mentions | umls-concept:C1706211 | lld:lifeskim |
| pubmed-article:11112509 | lifeskim:mentions | umls-concept:C0007961 | lld:lifeskim |
| pubmed-article:11112509 | lifeskim:mentions | umls-concept:C1546426 | lld:lifeskim |
| pubmed-article:11112509 | lifeskim:mentions | umls-concept:C1548280 | lld:lifeskim |
| pubmed-article:11112509 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:11112509 | pubmed:dateCreated | 2001-1-8 | lld:pubmed |
| pubmed-article:11112509 | pubmed:abstractText | We have created protein domains with extreme surface charge. These mutated domains allow for ion-exchange chromatography under conditions favourable for selective and efficient capture, using Escherichia coli as a host organism. The staphylococcal protein A-derived domain Z (Zwt) was used as a scaffold when constructing two mutants, Zbasic1 and Zbasic2, with high positive surface charge. Far-ultraviolet circular dichroism measurements showed that they have a secondary structure content comparable to the parental molecule Zwt. Although melting temperatures (Tm) of the engineered domains were lower than that of the wild-type Z domain, both mutants could be produced successfully as intracellular full-length products in E. coli and purified to homogeneity by ion-exchange chromatography. Further studies performed on Zbasic1 and Zbasic2 showed that they were able to bind to a cation exchanger even at pH values in the 9 to 11 range. A gene fusion between Zbasic2 and the acidic human serum albumin binding domain (ABD), derived from streptococcal protein G, was also constructed. The gene product Zbasic2-ABD could be purified using cation-exchange chromatography from a whole cell lysate to more than 90% purity. | lld:pubmed |
| pubmed-article:11112509 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11112509 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11112509 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11112509 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11112509 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11112509 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11112509 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11112509 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11112509 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11112509 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:11112509 | pubmed:issn | 0269-2139 | lld:pubmed |
| pubmed-article:11112509 | pubmed:author | pubmed-author:LundinGG | lld:pubmed |
| pubmed-article:11112509 | pubmed:author | pubmed-author:UhlénMM | lld:pubmed |
| pubmed-article:11112509 | pubmed:author | pubmed-author:HoberSS | lld:pubmed |
| pubmed-article:11112509 | pubmed:author | pubmed-author:NygrenP APA | lld:pubmed |
| pubmed-article:11112509 | pubmed:author | pubmed-author:GräslundTT | lld:pubmed |
| pubmed-article:11112509 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11112509 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:11112509 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11112509 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11112509 | pubmed:pagination | 703-9 | lld:pubmed |
| pubmed-article:11112509 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:11112509 | pubmed:meshHeading | pubmed-meshheading:11112509... | lld:pubmed |
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| pubmed-article:11112509 | pubmed:meshHeading | pubmed-meshheading:11112509... | lld:pubmed |
| pubmed-article:11112509 | pubmed:meshHeading | pubmed-meshheading:11112509... | lld:pubmed |
| pubmed-article:11112509 | pubmed:meshHeading | pubmed-meshheading:11112509... | lld:pubmed |
| pubmed-article:11112509 | pubmed:meshHeading | pubmed-meshheading:11112509... | lld:pubmed |
| pubmed-article:11112509 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11112509 | pubmed:articleTitle | Charge engineering of a protein domain to allow efficient ion-exchange recovery. | lld:pubmed |
| pubmed-article:11112509 | pubmed:affiliation | Department of Biotechnology, Royal Institute of Technology (KTH), S-100 44 Stockholm, Sweden. | lld:pubmed |
| pubmed-article:11112509 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11112509 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
