Abstract
The patterns of conformational changes induced in pig antibodies to 2,4-dinitrophenyllisin on binding with hapten were investigated by precise measurements of ultrasound velocity. It was shown that upon specific binding with intact antibodies, the observed slow changes of the bulk-clustic properties of the investigated solution reflect self-association of IgG molecules. In the case of interaction of Fab-fragments with hapten no changes of the acoustic properties were found. It was assumed that self-association is related to the increase in the hydrophobicity of Fe-fragments observed upon conformational changes of IgG molecules.
Translated title of the contribution | Study of antibody-hapten interaction by measuring velocity of ultrasound propagation |
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Original language | Russian |
Pages (from-to) | 572-575 |
Number of pages | 4 |
Journal | Biofizika |
Volume | 33 |
Issue number | 4 |
State | Published - Jul 1988 |