Small‐Angle X‐Ray Studies of the Human Immunoglobulin Molecule Kol

The conformation of the human immunoglobulin molecule Kol [IgG I, χ2γ2, Gm(f)+] was studied by small‐angle X‐ray scattering in 0.15 M NaCl solution. The radius of gyration was found to be 5.84 ± 0.04 nm, the volume 329 ± 15 nm3 and the molecular weight 150000 ± 10000. Information on the overall shap...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	European journal of biochemistry 1977-05, Vol.75 (1), p.195-199
Hauptverfasser:	PILZ, Ingrid, SCHWARZ, Erika, PALM, Walter
Format:	Artikel
Sprache:	eng
Schlagworte:	Female Humans Immunoglobulin G Immunoglobulin gamma-Chains Immunoglobulin kappa-Chains Models, Molecular Molecular Weight Multiple Myeloma - immunology Protein Conformation X-Ray Diffraction
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	The conformation of the human immunoglobulin molecule Kol [IgG I, χ2γ2, Gm(f)+] was studied by small‐angle X‐ray scattering in 0.15 M NaCl solution. The radius of gyration was found to be 5.84 ± 0.04 nm, the volume 329 ± 15 nm3 and the molecular weight 150000 ± 10000. Information on the overall shape was obtained by comparing the experimental scattering curve with the calculated curves for various models. The models were obtained by arranging the models found for the Fab and Fc fragments of the same immunoglobulin molecule in a different manner. A model which fits all the date and the form of the experimental scattering curve is presented.
ISSN:	0014-2956 1432-1033
DOI:	10.1111/j.1432-1033.1977.tb11517.x