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Structural and physicochemical analysis of the reaction between the anti-lysozyme antibody D1.3 and the anti-idiotopic antibodies E225 and E5.2

✍ Scribed by Diana Tello; Edward Eisenstein; Frederick P. Schwarz; Fernando A. Goldbaum; Barry A. Fields; Roy A. Mariuzza; Roberto J. Poljak

Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
595 KB
Volume
7
Category
Article
ISSN
0952-3499

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✦ Synopsis

Abstract

The reaction between the mouse (BALB/c) anti‐idiotiopic monoclonal antibodies E225 and E5.2 and idiotopes on the (BALB/c) anti‐lysozyme monoclonal antibody D1.3 has been characterized by titration calorimetry, by equilibrium sedimentation and by the determination of binding association and dissociation rates. The reaction between E5.2 and D1.3 is driven by a large negative enthalpy and its rate and equilibrium association constants are comparable to those observed in other antigen–antibody reactions. In contrast, the reaction between E225 and D1.3 is entropically driven and characterized by slow association kinetic (1 × 10^3^ M^−1^ sec^−1^) and a resulting low equilibrium constant (K~a~ = 2 × 10^5^M^−1^). A correlation of these properties with the three‐dimensional structure of the Fab225‐FabD1.3 complex, previously determined by X‐ray diffraction methods to 2.5 Å resolution, indicates that conformational changes of several D1.3 contacting residues, located in its complementarity determining regions, may explain these features of the reaction.

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