| pubmed-article:12018940 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12018940 | lifeskim:mentions | umls-concept:C0014653 | lld:lifeskim |
| pubmed-article:12018940 | lifeskim:mentions | umls-concept:C0042849 | lld:lifeskim |
| pubmed-article:12018940 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:12018940 | lifeskim:mentions | umls-concept:C0086024 | lld:lifeskim |
| pubmed-article:12018940 | lifeskim:mentions | umls-concept:C0242210 | lld:lifeskim |
| pubmed-article:12018940 | lifeskim:mentions | umls-concept:C0597731 | lld:lifeskim |
| pubmed-article:12018940 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:12018940 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:12018940 | pubmed:dateCreated | 2002-5-20 | lld:pubmed |
| pubmed-article:12018940 | pubmed:abstractText | Surface plasmon resonance biosensor analysis was used to evaluate the thermodynamics and binding kinetics of naturally occurring and synthetic cobalamins interacting with vitamin B(12) binding proteins. Cyanocobalamin-b-(5-aminopentylamide) was immobilized on a biosensor chip surface to determine the affinity of different cobalamins for transcobalamin, intrinsic factor, and nonintrinsic factor. A solution competition binding assay, in which a surface immobilized cobalamin analog competes with analyte cobalamin for B(12) protein binding, shows that only recombinant human transcobalamin is sensitive to modification of the corrin ring b-propionamide of cyanocobalamin. A direct binding assay, where recombinant human transcobalamin is conjugated to a biosensor chip, allows kinetic analysis of cobalamin binding. Response data for cyanocobalamin binding to the transcobalamin protein surface were globally fitted to a bimolecular interaction model that includes a term for mass transport. This model yields association and dissociation rate constants of k(a) = 3 x 10(7) M(-1) s(-1) and k(d) = 6 x 10(-4) s(-1), respectively, with an overall dissociation constant of K(D) = 20 pM at 30 degrees C. Transcobalamin binds cyanocobalamin-b-(5-aminopentylamide) with association and dissociation rates that are twofold slower and threefold faster, respectively, than transcobalamin binding to cyanocobalamin. The affinities determined for protein-ligand interaction, using the solution competition and direct binding assays, are comparable, demonstrating that surface plasmon resonance provides a versatile way to study the molecular recognition properties of vitamin B(12) binding proteins. | lld:pubmed |
| pubmed-article:12018940 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12018940 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12018940 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12018940 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12018940 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12018940 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12018940 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12018940 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12018940 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12018940 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12018940 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12018940 | pubmed:issn | 0003-2697 | lld:pubmed |
| pubmed-article:12018940 | pubmed:author | pubmed-author:AlpersDavid... | lld:pubmed |
| pubmed-article:12018940 | pubmed:author | pubmed-author:MyszkaDavid... | lld:pubmed |
| pubmed-article:12018940 | pubmed:author | pubmed-author:CannonMichell... | lld:pubmed |
| pubmed-article:12018940 | pubmed:author | pubmed-author:BagnatoJoshua... | lld:pubmed |
| pubmed-article:12018940 | pubmed:author | pubmed-author:WestFrederick... | lld:pubmed |
| pubmed-article:12018940 | pubmed:author | pubmed-author:GrissomCharle... | lld:pubmed |
| pubmed-article:12018940 | pubmed:copyrightInfo | (c) 2002 Elsevier Science (USA). | lld:pubmed |
| pubmed-article:12018940 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12018940 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12018940 | pubmed:volume | 305 | lld:pubmed |
| pubmed-article:12018940 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12018940 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12018940 | pubmed:pagination | 1-9 | lld:pubmed |
| pubmed-article:12018940 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12018940 | pubmed:meshHeading | pubmed-meshheading:12018940... | lld:pubmed |
| pubmed-article:12018940 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12018940 | pubmed:articleTitle | Equilibrium and kinetic analyses of the interactions between vitamin B(12) binding proteins and cobalamins by surface plasmon resonance. | lld:pubmed |
| pubmed-article:12018940 | pubmed:affiliation | Department of Chemistry, University of Utah, 315 S. 1400 E., Salt Lake City, UT 84112-0850, USA. | lld:pubmed |
| pubmed-article:12018940 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12018940 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12018940 | lld:pubmed |
