[Effect of dehydration on interdomain interactions in immunoglobulin G and its fragments].
Influence of urea on the structure of human IgG and isolated Fab and Fc-fragments was investigated by temperature-perturbation difference spectroscopy and circular dichroism. It was shown that 2M urea caused non-denaturational changes of IgG quaternary structure, localized in Fab-fragments. The same changes occur in solutions with ethylene glycol and glycerine as well. Apparently the main cause of these changes is dehydration. It is possible that the investigated effects model the conformational changes which appear in immunoglobulins after antigen binding.
D002942:Circular Dichroism; D003890:Desiccation; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D011487:Protein Conformation; D011489:Protein Denaturation; D013053:Spectrophotometry; D014364:Tryptophan; D014443:Tyrosine; D014508:Urea
D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007128:Immunoglobulin Fragments; D007074:Immunoglobulin G; D014443:Tyrosine; D014364:Tryptophan; D014508:Urea
Vliianie degidratatsii na mezhdomennye vzaimodeĭstviia v immunoglobuline G i ego fragmentakh.