Structure of human myeloma IgG3 Kuc

An electron microscopy study of human myeloma IgG3 Kuc has shown that the hinge region in an intact molecule is in a compact state. The subunits are not fixed rigidly and are very mobile. These data are supported by results of ultracentrifugation and microcalorimetry. Non‐extremal denaturating effec...

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Veröffentlicht in:	European journal of biochemistry 1990-06, Vol.190 (2), p.393-399
Hauptverfasser:	RYAZANTSEV, Sergey, TISHCHENKO, Vladimir, VASILIEV, Victor, ZAV'YALOV, Vladimir, ABRAMOV, Vyacheslav
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies, immunoglobulins Biological and medical sciences Freeze Drying Fundamental and applied biological sciences. Psychology Fundamental immunology Humans Hydrogen-Ion Concentration Immunoglobulin G - isolation & purification Immunoglobulin G - ultrastructure Immunoglobulin Variable Region - physiology Microscopy, Electron Molecular immunology Monoclonal antibodies Multiple Myeloma - immunology Protein Conformation Protein Denaturation Staining and Labeling Temperature Ultracentrifugation
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Beschreibung
Zusammenfassung:	An electron microscopy study of human myeloma IgG3 Kuc has shown that the hinge region in an intact molecule is in a compact state. The subunits are not fixed rigidly and are very mobile. These data are supported by results of ultracentrifugation and microcalorimetry. Non‐extremal denaturating effects (pH 4.0, 20°C or pH 7.8, 65°C) lead to ‘unfolding’ of the hinge region which has a rod‐like shape in electron micrographs.
ISSN:	0014-2956 1432-1033
DOI:	10.1111/j.1432-1033.1990.tb15588.x