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Folding of the Fab fragment within the intact antibody
Author(s) -
Lilie Hauke
Publication year - 1997
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/s0014-5793(97)01293-3
Subject(s) - chemistry , immunoglobulin fab fragments , antibody , fragment (logic) , denaturation (fissile materials) , kinetics , immunoglobulin fc fragments , immunoglobulin g , biochemistry , biophysics , peptide sequence , complementarity determining region , biology , immunology , physics , quantum mechanics , nuclear chemistry , computer science , gene , programming language
At present it is not clear to which extent the Fab fragment and the Fc part of an antibody interact in the intact immunoglobulin structure. To determine such potential interactions the unfolding and refolding of an isolated Fab fragment and the respective antibody MAK 33 (κ/IgG1) are compared. It could be shown that the proline independent renaturation kinetics of both an unfolding intermediate and the fully denatured form of both proteins are identical. Upon denaturation, the loss of antigen binding activity occurs with the same rate for both the Fab fragment and the intact antibody. However, the complete structural unfolding of the Fab part of the antibody is significantly slower than that of the isolated Fab fragment. These kinetic data suggest that the structure of the Fab fragment within the intact antibody is stabilized by interactions, presumably with the Fc part, missing in the isolated Fab.