| pubmed-article:1597185 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1597185 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1597185 | lifeskim:mentions | umls-concept:C1548779 | lld:lifeskim |
| pubmed-article:1597185 | lifeskim:mentions | umls-concept:C1947902 | lld:lifeskim |
| pubmed-article:1597185 | lifeskim:mentions | umls-concept:C0303920 | lld:lifeskim |
| pubmed-article:1597185 | lifeskim:mentions | umls-concept:C2827499 | lld:lifeskim |
| pubmed-article:1597185 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:1597185 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:1597185 | lifeskim:mentions | umls-concept:C1167624 | lld:lifeskim |
| pubmed-article:1597185 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1597185 | pubmed:dateCreated | 1992-7-7 | lld:pubmed |
| pubmed-article:1597185 | pubmed:abstractText | A cleavable cross-linking reagent, sulfosuccinimidyl-2(7-azido-4-methylcoumarin-3-acetamido)-ethyl-1,3'- dithiopropionate (SAED), was synthesized for the selective transfer of a coumarin fluorophore from a 'donor' protein to a position near the binding site of an interacting 'target' protein. SAED contains a terminal N-sulfosuccinimidyl ester for conjugation to the donor, a terminal photoactivatable azido-coumarin species for cross-linking with the interacting target, and a central disulfide spacer for the release of the labeled target after cleavage. To evaluate the effectiveness of this labeling reagent, soybean trypsin inhibitor (STI) was derivatized (approximately 0.5 mol/mol) with SAED and then photolyzed in the presence of trypsin. A single fluorescent cross-linked species (6-7 mol% of total STI) was observed by SDS/PAGE and, after reductive cleavage, was shown to be a 1:1 STI-trypsin complex. This complex was not detected without photolysis or with an inactivated cross-linker. Importantly, complex formation was inhibited by an excess of unmodified STI and prevented by substitution of a non-interacting protein for trypsin. Cleavage of the cross-linked complex revealed that the trypsin, but not the STI, was fluorescent; the uncomplexed trypsin fraction remained unlabeled. These results demonstrated the specificity of the labeling of trypsin by fluorescent-transfer cross-linking with SAED. An efficiency of about 15% for this cross-linking mediated labeling of trypsin was calculated. The short cross-linking span of SAED (less than or equal to 1.8 nm) strictly limited the labeling to the vicinity of the contact region of trypsin with STI. Thus, this novel cross-linker permits the region-specific targeting of a fluorophore near a functionally important binding site. | lld:pubmed |
| pubmed-article:1597185 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1597185 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1597185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1597185 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1597185 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:1597185 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:1597185 | pubmed:author | pubmed-author:ShohetS BSB | lld:pubmed |
| pubmed-article:1597185 | pubmed:author | pubmed-author:IkemotoNN | lld:pubmed |
| pubmed-article:1597185 | pubmed:author | pubmed-author:KaneJ LJL | lld:pubmed |
| pubmed-article:1597185 | pubmed:author | pubmed-author:ShahrokhZZ | lld:pubmed |
| pubmed-article:1597185 | pubmed:author | pubmed-author:TheveninB JBJ | lld:pubmed |
| pubmed-article:1597185 | pubmed:author | pubmed-author:FujimotoE KEK | lld:pubmed |
| pubmed-article:1597185 | pubmed:author | pubmed-author:WilliardR LRL | lld:pubmed |
| pubmed-article:1597185 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1597185 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1597185 | pubmed:volume | 206 | lld:pubmed |
| pubmed-article:1597185 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1597185 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1597185 | pubmed:pagination | 471-7 | lld:pubmed |
| pubmed-article:1597185 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
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| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:meshHeading | pubmed-meshheading:1597185-... | lld:pubmed |
| pubmed-article:1597185 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1597185 | pubmed:articleTitle | A novel photoactivatable cross-linker for the functionally-directed region-specific fluorescent labeling of proteins. | lld:pubmed |
| pubmed-article:1597185 | pubmed:affiliation | Department of Medicine, University of California, San Francisco 94143. | lld:pubmed |
| pubmed-article:1597185 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1597185 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1597185 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
