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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lancet, D. Pecht, I. |
| Abstract | The kinetics of hapten binding to the homogeneous immunoglobulin A secreted by the murine plasmacytoma MOPC 460 was investigated by the chemical relaxation method. Two distinct relaxation times were observed in the binding equilibrium with three different haptens. A detailed concentration dependence analysis of relaxation times and amplitudes was performed with the hapten epsilon-N(2,4-dinitrophenyl)-lysine (Dnp-Lys). The results support a mechanism in which two interconvertible conformational states of the protein bind the hapten with different association constants. Hapten binding shifts the equilibrium towards the better binding state. These observations form kinetic evidence for a conformational transition induced in the immunoglobulin by ligand binding to its antigen binding site, and are in line with the allosteric hypothesis for the initiation of physiological functions by antigen-antibody association. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 10 |
| Volume Number | 73 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1976-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Dinitrobenzenes Pharmacology Haptens Immunoglobulin A Myeloma Proteins Nitrobenzenes Allosteric Regulation Antigen-Antibody Reactions Binding Sites, Antibody Metabolism Kinetics Ligands Protein Conformation Drug Effects Temperature Thermodynamics Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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