Relations between macro- and microstability of CH2 domains and human IgG2 and their biological activity: 1. Analysis of calorimetric and optical melting curves

In this study, we examined the human myeloma second-class immunoglobulins, LOM and SIN, and their Fc fragments, by a number of physical methods, such as scanning calorimetry, fluorescence spectroscopy and analytical centrifugation. In addition, we obtained and carried out a separate analysis of thei...

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Bibliographic Details
Published in:Molecular biology (New York) 2014, Vol.48 (3), p.414-423
Main Author: Tishchenko, V. M.
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Human Genetics
Life Sciences
Structural and Functional Analysis of Biopolymers and Biopolymer Complexes
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Summary:In this study, we examined the human myeloma second-class immunoglobulins, LOM and SIN, and their Fc fragments, by a number of physical methods, such as scanning calorimetry, fluorescence spectroscopy and analytical centrifugation. In addition, we obtained and carried out a separate analysis of their hFc fragments, which contain not only the lower portion of the hinge region, but its complete core peptide, Cys-Cys-Val-Glu-Cys-Pro-Pro-Cys. Joint analysis of calorimetric and optical melting curves revealed that only the first low-temperature heat absorption peak in all of the melting curves corresponded to the melting of the two C H 2 domains. Thus, we demonstrate that the C H 2 domains of the intact IgG2 are present in a less compact conformation compared to their state within the hFc and Fc fragments.
ISSN:0026-8933
1608-3245
DOI:10.1134/S0026893314030200