pubmed-article:999647 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C0026794 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C0449445 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C0205431 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C0205117 | lld:lifeskim |
pubmed-article:999647 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:999647 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:999647 | pubmed:dateCreated | 1977-1-25 | lld:pubmed |
pubmed-article:999647 | pubmed:abstractText | We have previously shown that an antigenic site in native lysozyme resides around the disulphide bridge 30-115 and incorporates Lys-33 and Lys-116 and one or both of Tyr-20 and Tyr-23. These residues fall in an imaginary line circumscribing part of the surface of the molecule and passing through the spatially adjacent residues Tyr-20, Arg-21, Tyr-23, Lys-116, Asn-113, Arg-114, Phe-34 and Lys-33. The identity of the site was confirmed by demonstrating that the synthetic peptide Tyr-Arg-Tyr-Gly-Lys-Asn-Arg-Gly-Phe-Lys (which does not exist in lysozyme but simulates a surface region of it), and an analogue in which glycine replaced Tyr-23, possessed remarkable immuno-chemical reactivity that accounted entirely for the expected reactivity of the site in native lysozyme. Tyr-23 is not part of the site, and its contribution was satisfied by a glycine spacer. The novel approach presents a powerful technique for the delineation of antigenic (and other binding) sites in native proteins and confirms that these need not always comprise residues in direct peptide linkage. | lld:pubmed |
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pubmed-article:999647 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:999647 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:999647 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:999647 | pubmed:language | eng | lld:pubmed |
pubmed-article:999647 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:999647 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:999647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:999647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:999647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:999647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:999647 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:999647 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:999647 | pubmed:month | Oct | lld:pubmed |
pubmed-article:999647 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:999647 | pubmed:author | pubmed-author:AtassiM ZMZ | lld:pubmed |
pubmed-article:999647 | pubmed:author | pubmed-author:LeaC HCH | lld:pubmed |
pubmed-article:999647 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:999647 | pubmed:day | 1 | lld:pubmed |
pubmed-article:999647 | pubmed:volume | 159 | lld:pubmed |
pubmed-article:999647 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:999647 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:999647 | pubmed:pagination | 89-93 | lld:pubmed |
pubmed-article:999647 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:999647 | pubmed:meshHeading | pubmed-meshheading:999647-A... | lld:pubmed |
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pubmed-article:999647 | pubmed:meshHeading | pubmed-meshheading:999647-P... | lld:pubmed |
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pubmed-article:999647 | pubmed:meshHeading | pubmed-meshheading:999647-A... | lld:pubmed |
pubmed-article:999647 | pubmed:meshHeading | pubmed-meshheading:999647-B... | lld:pubmed |
pubmed-article:999647 | pubmed:year | 1976 | lld:pubmed |
pubmed-article:999647 | pubmed:articleTitle | Delineation of the third antigenic site of lysozyme by application of a novel 'surface-simulation' synthetic approach directly linking the conformationally adjacent residues forming the site. | lld:pubmed |
pubmed-article:999647 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:999647 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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