Linked Life Data

3398861

Source:http://linkedlifedata.com/resource/pubmed/id/3398861

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-9-6
pubmed:abstractText
The binding thermodynamics of seven different oligosaccharide haptens to the dextran-specific IgM secreted by the murine plasmacytoma MOPC-104E were studied by direct calorimetric measurements. The enthalpy change values observed for the binding process range between -5 and -16 kcal/mol depending on the hapten and the temp of measurement. The antibody-hapten interactions were characterized by a positive heat capacity change [delta Cp approximately 300 cal/(mol.degree)] and a resultant process of enthalpy-entropy compensation. The calculated change in unitary entropy of the reaction, delta Su, ranged between -20 and -30 eu (4 degrees C), corresponding to an expected entropy loss due to immobilization of the hapten molecules. The entropy of binding increased with rising temp, thus compensating for the decreasing enthalpy contribution to the free energy of binding. The data are consistent with a hapten binding induced conformational transition to a more relaxed state in the immunoglobulin molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
379-83
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Thermodynamics of oligosaccharides binding to a dextran-specific monoclonal IgM.
pubmed:affiliation
Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
pubmed:publicationType
Journal Article