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Comparative thermodynamic analyses of the Fv, Fab* and Fab and Fab fragments of anti‐dansyl mouse monoclonal antibody
Author(s) -
Nobuhisa Shimba,
Hidetaka Torigoe,
Hideo Takahashi,
Koichi Masuda,
Ichio Shimada,
Yoshiaki Arata,
Akinori Sarai
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00113-n
Subject(s) - chemistry , monoclonal antibody , antigen , immunoglobulin fab fragments , antibody , stereochemistry , microbiology and biotechnology , peptide sequence , biochemistry , complementarity determining region , biology , immunology , gene
In order to investigate the role of the constant domainson 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, enthalphy 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.