Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low pH-induced state

Thermodynamic and functional characterization of a stable IgG conformer obtained by renaturation from a partially structured low pH-induced state

At pH 2, rabbit IgG adopts a partially structured state that exhibits loss of thermal unfolding transition, tentatively assigned to the CH2 domain, whilst retaining a well-defined tertiary structure for the rest of the molecule and extensive secondary structure. Renaturation of IgG from this state y...

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Bibliographic Details
Published in:FEBS letters Vol. 361; no. 2; pp. 173 - 175
Main Authors: Martsev, Sergey P., Kravchuk, Zinaida I., Vlasov, Alexander P., Lyakhnovich, Georgy V.
Format: Journal Article
Language:English
Published: England Elsevier B.V 20-03-1995
Subjects:
Animals
C1q component of complement
Conformational probe
Differential scanning calorimetry
Ferritins - immunology
Humans
Hydrogen-Ion Concentration
IgG conformer
Immunoglobulin
Immunoglobulin G - chemistry
Protein Conformation
Protein Denaturation
Protein Structure, Secondary
Protein Structure, Tertiary
Rabbits
Thermodynamics
Differential scanning calorimetry
Conformational probe
Immunoglobulin
C1q component of complement
IgG conformer
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Summary:At pH 2, rabbit IgG adopts a partially structured state that exhibits loss of thermal unfolding transition, tentatively assigned to the CH2 domain, whilst retaining a well-defined tertiary structure for the rest of the molecule and extensive secondary structure. Renaturation of IgG from this state yields a stable conformer that differs from native IgG by a lower degree of interaction between the CH2 and CH3 domains, and stronger interaction between the CH1 and CH2 domains, as judged by differential scanning calorimetry and probing the IgG conformation with specific ligands (C1q component of complement, protein A and monospecific antibodies to the CH2 domain and hinge region).
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00145-Y