Linked Life Data

15047907

Source:http://linkedlifedata.com/resource/pubmed/id/15047907

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pubmed-article:15047907pubmed:abstractTextFluorescein and its analogs are among the best fluorophores to label proteins and the labeling generally involves chemical modification of a translated protein. Using this methodology, labeling at a specific position remains difficult. It is known that the guinea pig liver transglutaminase (TGase)-catalyzed enzymatic modification method can allow terminal-specific fluorophore labeling of a protein by monodansylcadaverine. However, native activity of the fluorescent protein has not been investigated so far, nor has direct comparison between the chemical modification and the TGase-catalyzed modification been attempted. Therefore, we compared the possibility of fluorescein labeling via chemical labeling and via TGase-catalyzed modification. The latter method was found to be very practical and overcame some of the problems associated with the specificity of the former; fluorescein was covalently attached only to the N- or C-terminal site of glutathione S-transferase when the reaction was catalyzed by TGase and the resulting labeled protein completely retained its native activity. The TGase-mediated labeling occurred not only at room temperature but also at 4 degrees C to the same extent, which is more desirable for preventing the inactivation of proteins.lld:pubmed
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pubmed-article:15047907pubmed:authorpubmed-author:TairaKazunari...lld:pubmed
pubmed-article:15047907pubmed:authorpubmed-author:TakiMasumiMlld:pubmed
pubmed-article:15047907pubmed:authorpubmed-author:ShiotaMakiMlld:pubmed
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pubmed-article:15047907pubmed:volume17lld:pubmed
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pubmed-article:15047907pubmed:pagination119-26lld:pubmed
pubmed-article:15047907pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15047907pubmed:year2004lld:pubmed
pubmed-article:15047907pubmed:articleTitleTransglutaminase-mediated N- and C-terminal fluorescein labeling of a protein can support the native activity of the modified protein.lld:pubmed
pubmed-article:15047907pubmed:affiliationDepartment of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Hongo, Tokyo 113-8656, Japan.lld:pubmed
pubmed-article:15047907pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:15047907pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:15047907pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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