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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-3-29
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pubmed:abstractText |
The commonly used purification procedures for Transferrin-binding protein B (TbpB) are based on an affinity chromatography step using resins onto which human transferrin had been immobilized. These protocols involve protein elution using denaturing buffer solutions. Here we present an improved protocol which permits protein elution under nondenaturing conditions using chelating agents such as phosphate or compounds containing a pyrophosphate group. Furthermore, isothermal titration calorimetry experiments of the purified protein with holotransferrin have been shown to be a reliable method to assess the purity and activity of the purified material.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1046-5928
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2002 Elsevier Science (USA).
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pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
323-8
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pubmed:dateRevised |
2002-12-13
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pubmed:meshHeading |
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pubmed:year |
2002
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pubmed:articleTitle |
Affinity-purification of Transferrin-binding protein B under nondenaturing conditions.
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pubmed:affiliation |
Aventis Pasteur, 1541 avenue Marcel Mérieux, 69280 Marcy l'Etoile, France. tino.krell@aventis.com
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pubmed:publicationType |
Journal Article
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