pubmed-article:2183792 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2183792 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:2183792 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
pubmed-article:2183792 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:2183792 | lifeskim:mentions | umls-concept:C0075289 | lld:lifeskim |
pubmed-article:2183792 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:2183792 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2183792 | pubmed:dateCreated | 1990-5-16 | lld:pubmed |
pubmed-article:2183792 | pubmed:abstractText | The gene for Protein G from Streptococcus strain G148 was cloned and expressed in Escherichia coli. The regions on the gene corresponding to the albumin-binding domains and the Fab-binding region were then deleted by site-directed mutagenesis. The translation of regions corresponding to the cell-wall- and membrane-binding domains was prevented by introduction of stop codons upstream of these domains. This recombinant DNA sequence codes for a protein (G') that contains repetitive regions and that binds only the Fc portion of IgG, analogously to Protein A. Translation of the sequence produces a protein with an Mr of about 20,000. The nucleotide sequence differs from those published previously [Guss, Eliasson, Olsson, Uhlén, Frej, Jornvall, Flock & Lindberg (1986) EMBO J. 5, 1567-1575; Olsson, Eliasson, Guss, Nilsson, Hellman, Lindberg & Uhlén (1987) Eur. J. Biochem. 168, 319-324]. The protein can be substantially purified on a large scale by chromatography on IgG-Sepharose 4B. Homogeneous Protein G' can be prepared by anion-exchange f.p.l.c. on Mono Q HR. This Protein G' has a pI of 4.19 and SDS/PAGE gives an apparent anomalous Mr of 35,000. | lld:pubmed |
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pubmed-article:2183792 | pubmed:language | eng | lld:pubmed |
pubmed-article:2183792 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2183792 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2183792 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2183792 | pubmed:month | Apr | lld:pubmed |
pubmed-article:2183792 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:2183792 | pubmed:author | pubmed-author:AtkinsonTT | lld:pubmed |
pubmed-article:2183792 | pubmed:author | pubmed-author:MurphyJ PJP | lld:pubmed |
pubmed-article:2183792 | pubmed:author | pubmed-author:GowardC RCR | lld:pubmed |
pubmed-article:2183792 | pubmed:author | pubmed-author:BarstowD ADA | lld:pubmed |
pubmed-article:2183792 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2183792 | pubmed:day | 1 | lld:pubmed |
pubmed-article:2183792 | pubmed:volume | 267 | lld:pubmed |
pubmed-article:2183792 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2183792 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2183792 | pubmed:pagination | 171-7 | lld:pubmed |
pubmed-article:2183792 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2183792 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2183792 | pubmed:articleTitle | Expression and purification of a truncated recombinant streptococcal protein G. | lld:pubmed |
pubmed-article:2183792 | pubmed:affiliation | Division of Biotechnology, PHLS Centre for Applied Microbiology and Research, Salisbury, Wilts, U.K. | lld:pubmed |
pubmed-article:2183792 | pubmed:publicationType | Journal Article | lld:pubmed |
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