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rdf:type |
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lifeskim:mentions |
umls-concept:C0003241,
umls-concept:C0007952,
umls-concept:C0014442,
umls-concept:C0205099,
umls-concept:C0205217,
umls-concept:C0205419,
umls-concept:C0205681,
umls-concept:C0332120,
umls-concept:C0524637,
umls-concept:C0600499,
umls-concept:C1550024,
umls-concept:C1554080,
umls-concept:C1706198,
umls-concept:C1710236
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pubmed:issue |
Pt 1
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pubmed:dateCreated |
2004-6-21
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pubmed:abstractText |
The substrate selectivities of an anti-phosphonate and an anti-phosphate kinetically homogeneous polyclonal catalytic antibody preparation and two hydrolytic enzymes were compared by using hapten-analogous and truncated carbonate and ester substrates each containing a 4-nitrophenolate leaving group. Syntheses of the truncated substrates devoid of recognition features in the non-leaving group parts of the substrates are reported. The relatively high kinetic selectivity of the more active anti-phosphonate antibody preparation is considered to depend on a relatively rigid catalytic site with substantial reaction centre specificity together with other important recognition interactions with the extended non-leaving group part of the substrate. In contrast, the less catalytically active, more flexible anti-phosphate antibody exhibits much lower kinetic selectivity for the substrate reaction centre comparable with that of the hydrolytic enzymes with activity much less dependent on recognition interactions with the non-leaving group part of the substrate. The ways in which haptenic flexibility and IgG architecture might contribute to the differential kinetic selectivities are indicated.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-10657247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-10722164,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-10887904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-11384190,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-11439083,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-12379360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-12643810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-12946271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-13909163,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-1953683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-2276457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-2730566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-3372492,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-4455211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-4854723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-4981346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-7536111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-7760931,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-7809611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-8114766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-9027317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-9180069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-9223277,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-9337880,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15053743-9878416
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1470-8728
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pubmed:author |
pubmed-author:BoucherGuillaumeG,
pubmed-author:BrocklehurstKeithK,
pubmed-author:Flórez-OlvarezJoséJ,
pubmed-author:GallacherGerardG,
pubmed-author:GulSherazS,
pubmed-author:HussainSyeedS,
pubmed-author:OstlerElizabeth LEL,
pubmed-author:ResminiMarinaM,
pubmed-author:SaidBilalB,
pubmed-author:SonkariaSanjivS,
pubmed-author:ThomasEmrys WEW
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
381
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
125-30
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15053743-Animals,
pubmed-meshheading:15053743-Antibodies, Catalytic,
pubmed-meshheading:15053743-Antibody Affinity,
pubmed-meshheading:15053743-Antigen-Antibody Reactions,
pubmed-meshheading:15053743-Binding Sites, Antibody,
pubmed-meshheading:15053743-Catalytic Domain,
pubmed-meshheading:15053743-Cattle,
pubmed-meshheading:15053743-Chymotrypsin,
pubmed-meshheading:15053743-Esterases,
pubmed-meshheading:15053743-Hydrolases,
pubmed-meshheading:15053743-Hydrolysis,
pubmed-meshheading:15053743-Liver,
pubmed-meshheading:15053743-Models, Molecular,
pubmed-meshheading:15053743-Pancreas,
pubmed-meshheading:15053743-Phosphates,
pubmed-meshheading:15053743-Phosphonic Acids,
pubmed-meshheading:15053743-Substrate Specificity,
pubmed-meshheading:15053743-Swine,
pubmed-meshheading:15053743-Vaccines, Synthetic
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pubmed:year |
2004
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pubmed:articleTitle |
Evidence for 'lock and key' character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes.
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pubmed:affiliation |
Laboratory of Structural and Mechanistic Enzymology, School of Biological Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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