Comparative thermodynamic analyses of the Fv, Fab* and Fab fragments of anti-dansyl mouse monoclonal antibody.
In order to investigate the role of the constant domains on the antigen-binding property of the variable domains, we have carried out a comparative thermodynamic study of the anti-dansyl Fv, Fab* and Fab fragments that possess the identical amino acid sequence of the variable domains. The thermodynamic analyses have shown that binding constants, enthalpy changes and entropy changes are similar for the three antigen-binding fragments, whereas the thermal stability of Fab is much higher than that of Fv and Fab*. We have concluded that (i) the variable domains of the three antigen-binding fragments possess identical intrinsic capability for antigen binding and (ii) the two constant domains serve to improve the stability of the variable domains.
Shimba
N
N
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Torigoe
H
H
Takahashi
H
H
Masuda
K
K
Shimada
I
I
Arata
Y
Y
Sarai
A
A
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry; D000937:Antigen-Antibody Reactions; D002152:Calorimetry, Differential Scanning; D003619:Dansyl Compounds; D007127:Immunoglobulin Constant Regions / Q000737:chemistry; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry*; D007128:Immunoglobulin Fragments / Q000737:chemistry*; D051379:Mice; D011485:Protein Binding; D011489:Protein Denaturation; D013816:Thermodynamics
D000911:Antibodies, Monoclonal; D003619:Dansyl Compounds; D007127:Immunoglobulin Constant Regions; D007140:Immunoglobulin Fab Fragments; D007128:Immunoglobulin Fragments; C055966:immunoglobulin Fv