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|
|Number of pages||4|
|State||Published - Jul 1988|