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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
Author(s) -
Tello Diana,
Eisenstein Edward,
Schwarz Frederick P.,
Goldbaum Fernando A.,
Fields Barry A.,
Mariuzza Roy A.,
Poljak Roberto J.
Publication year - 1994
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300070108
Subject(s) - lysozyme , antibody , chemistry , biochemistry , immunology , biology
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.