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Updated: Aug 19, 2026
Differential Scanning Calorimetry — A Method for Assessing the Thermal Stability and Conformation of Protein Antigen
Published on: March 4, 2017
Comparative study of monoclonal immunoglobulin M and rheumatoid immunoglobulin M by differential scanning
I I Protasevich1, B Ranjbar, Varlamova EYu
1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Abstract:
Thermal denaturation of monoclonal immunoglobulin M (IgM) and rheumatoid immunoglobulin M (IgM-RF) and their Fab- and (Fc)5-fragments was studied by differential scanning microcalorimetry. The melting of IgM-RF started at a higher temperature than that of IgM and the maximum temperature of its main asymmetric peak of heat absorption was higher by 4 degrees C. At equal values of enthalpy, the thermal denaturation of IgM-RF and IgM consisted of four and five individual transitions, respectively, between pairs of states. The comparison of thermal denaturation parameters of Fab- and (Fc)5-fragments of IgM-RF and IgM showed a thermodynamic similarity of (Fc)5-fragments of both proteins, while their Fab-fragments differed in the interaction between VL-CL and VH-CH domains.
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