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

FEBS Letters

Lyakhnovich, Georgy V.¹  Martsev, Sergey P.²  Vlasov, Alexander P.²  Kravchuk, Zinaida I.² 

[1] Institute of Photobiology, Skoriny Prosp. 27, Minsk 220733, Belarus;Institute of Bioorganic Chemistry, Academy of Sciences of Belarus, Zhodinskaya 5/2, Minsk 220141, Belarus

关键词: Immunoglobulin;    IgG conformer;    Differential scanning calorimetry;    Conformational probe;    C1q component of complement;   

DOI  :  10.1016/0014-5793(95)00145-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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).

【 授权许可】

Unknown