pubmed-article:2344038 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2344038 | lifeskim:mentions | umls-concept:C0014898 | lld:lifeskim |
pubmed-article:2344038 | lifeskim:mentions | umls-concept:C0184661 | lld:lifeskim |
pubmed-article:2344038 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
pubmed-article:2344038 | lifeskim:mentions | umls-concept:C1524063 | lld:lifeskim |
pubmed-article:2344038 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:2344038 | pubmed:dateCreated | 1990-6-27 | lld:pubmed |
pubmed-article:2344038 | pubmed:abstractText | A two-step zero-length crosslinking procedure for studying protein-protein complexes has been developed. One component of a complex is briefly incubated with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) in the presence of N-hydroxysuccinimide resulting in the conversion of some of the protein carboxyls into succinimidyl esters. The reaction is stopped by addition of beta-mercaptoethanol and other interacting proteins are then added. Crosslinking arises from substitution of lysine epsilon-amino groups of these proteins for the succinimidyl moieties during a 1- to 2-h incubation period. The advantage of this method versus one-step zero-length crosslinking is that only one component of the complex is exposed to the crosslinker, which eliminates complications arising from the formation of crosslinks among several proteins of a multicomponent complex. Furthermore, crosslinks can be formed even in the presence of reagents, such as dithiothreitol and EDTA, that would interfere with direct crosslinking with EDC. | lld:pubmed |
pubmed-article:2344038 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2344038 | pubmed:language | eng | lld:pubmed |
pubmed-article:2344038 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2344038 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2344038 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2344038 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2344038 | pubmed:month | Feb | lld:pubmed |
pubmed-article:2344038 | pubmed:issn | 0003-2697 | lld:pubmed |
pubmed-article:2344038 | pubmed:author | pubmed-author:GergelyJJ | lld:pubmed |
pubmed-article:2344038 | pubmed:author | pubmed-author:GrabarekZZ | lld:pubmed |
pubmed-article:2344038 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2344038 | pubmed:day | 15 | lld:pubmed |
pubmed-article:2344038 | pubmed:volume | 185 | lld:pubmed |
pubmed-article:2344038 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2344038 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2344038 | pubmed:pagination | 131-5 | lld:pubmed |
pubmed-article:2344038 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:2344038 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2344038 | pubmed:articleTitle | Zero-length crosslinking procedure with the use of active esters. | lld:pubmed |
pubmed-article:2344038 | pubmed:affiliation | Department of Muscle Research, Harvard Medical School, Massachusetts. | lld:pubmed |
pubmed-article:2344038 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2344038 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2344038 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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