[Interaction between CH2 and CH3-domains of human immunoglobulin G1 in glycosylated and aglycosylated Fc-fragments].
Heat denaturation of glycosylated and aglycosylated human immunoglobulin G1 Fc fragments was investigated by differential scanning microcalorimetry. The enthalpy of the interaction between aglycosylated CH2 and CH3 domains is significantly reduced at 37 degrees C (but not at 0 degree C) as compared to the glycosylated form. The temperature dependence is consistent with the data on restricted proteolysis by trypsin.
Tishchenko
V M
VM
Institute of Immunology, Lyubuchany, Moscow Region, Russia.
D002152:Calorimetry, Differential Scanning; D006031:Glycosylation; D006358:Hot Temperature; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry*; D007074:Immunoglobulin G / Q000737:chemistry*; D011489:Protein Denaturation; D013816:Thermodynamics
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G