The unfolding/denaturation of immunogammaglobulin of isotype 2b and its F(ab) and F(c) fragments.
The unfolding and further denaturation of IgG and its F(ab) and F(c) fragments were studied both on a macroscopic and molecular level, using differential scanning calorimetry and circular dichroism spectroscopy, respectively. It was shown that the structural integrity of the F(ab) and F(c) units was retained after fragmentation of the IgG. The F(ab) fragment denatured at approximately 61 degrees C and the F(c) fragment at 71 degrees C. The structural transitions observed in the whole IgG is the sum effect of those determined for the isolated F(ab) and F(c) fragments.
Vermeer
A W
AW
Laboratory for Physical Chemistry and Colloid Science, Wageningen University, 6703 HB Wageningen, The Netherlands. Ronald.Vermeer.rv@bayer-ag.de
Norde
W
W
van Amerongen
A
A
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry; D055592:Biophysical Phenomena; D001703:Biophysics; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry* / Q000302:isolation & purification; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry* / Q000302:isolation & purification; D007074:Immunoglobulin G / Q000737:chemistry*; D051379:Mice; D010206:Papain; D011489:Protein Denaturation; D017510:Protein Folding; D013696:Temperature
D000911:Antibodies, Monoclonal; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D010206:Papain