Advanced analyses of kinetic stabilities of iggs modified by mutations and glycosylation.

ABSTRACT: The stability of Immunoglobulin G (IgG) affects production, storage and usability, especially in the clinic. The complex thermal and isothermal transitions of IgGs, especially their irreversibilities, pose a challenge to the proper determination of parameters describing their thermodynamic and kinetic stability. Here, we present a reliable mathematical model to study the irreversible thermal denaturations of antibody variants. The model was applied to two unrelated IgGs and their variants with stabilizing mutations as well as corresponding non-glycosylated forms of IgGs and Fab fragments. Thermal denaturations of IgGs were analyzed with three transitions, one reversible transition corresponding to C(H)2 domain unfolding followed by two consecutive irreversible transitions corresponding to

SUBMITTER: Sedlak E 

PROVIDER: S-EPMC4500310 | biostudies-literature | 2015 Jul

REPOSITORIES: biostudies-literature