| pubmed-article:2249655 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2249655 | lifeskim:mentions | umls-concept:C0327698 | lld:lifeskim |
| pubmed-article:2249655 | lifeskim:mentions | umls-concept:C0001044 | lld:lifeskim |
| pubmed-article:2249655 | lifeskim:mentions | umls-concept:C0034760 | lld:lifeskim |
| pubmed-article:2249655 | lifeskim:mentions | umls-concept:C1510827 | lld:lifeskim |
| pubmed-article:2249655 | lifeskim:mentions | umls-concept:C1710234 | lld:lifeskim |
| pubmed-article:2249655 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:2249655 | pubmed:dateCreated | 1991-1-11 | lld:pubmed |
| pubmed-article:2249655 | pubmed:abstractText | Several peptides of acetylcholinesterase of Torpedo californica labelled with the alkylating reagent [3H]N,N-dimethyl-2-phenyl-aziridinium (DPA) were localized within the primary structure. One peptide had the sequence KPQELIDVE (positions 270-278); the incorporation of DPA into this peptide could be specifically suppressed by propidium, which suggests that it is part of the peripheral anionic site. The incorporation of DPA into two other peptides was insensitive to propidium but could be prevented by edrophonium; the sequence of one of the peptides assumed to be part of the anionic site in the catalytic centre was found to be DLFR (positions 217-220). Decamethonium efficiently blocked alkylation by DPA in all three investigated peptides. | lld:pubmed |
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| pubmed-article:2249655 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2249655 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2249655 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2249655 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2249655 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:2249655 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:2249655 | pubmed:author | pubmed-author:AaviksaarAA | lld:pubmed |
| pubmed-article:2249655 | pubmed:author | pubmed-author:HuchoFF | lld:pubmed |
| pubmed-article:2249655 | pubmed:author | pubmed-author:WeissUU | lld:pubmed |
| pubmed-article:2249655 | pubmed:author | pubmed-author:RabaRR | lld:pubmed |
| pubmed-article:2249655 | pubmed:author | pubmed-author:KreienkampH... | lld:pubmed |
| pubmed-article:2249655 | pubmed:author | pubmed-author:PedakAA | lld:pubmed |
| pubmed-article:2249655 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2249655 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:2249655 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2249655 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2249655 | pubmed:pagination | 3885-8 | lld:pubmed |
| pubmed-article:2249655 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2249655 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2249655 | pubmed:articleTitle | Anionic subsites of the acetylcholinesterase from Torpedo californica: affinity labelling with the cationic reagent N,N-dimethyl-2-phenyl-aziridinium. | lld:pubmed |
| pubmed-article:2249655 | pubmed:affiliation | Universität Berlin, Institut für Biochemie, FRG. | lld:pubmed |
| pubmed-article:2249655 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2249655 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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