Electron microscopy study of human myeloma immunoglobulin G1

Electron microscopy study of human myeloma immunoglobulin G1

Human immunoglobulin G1 Van was studied by negative staining, freeze drying and high resolution shadow casting. The Fab and Fe subunits of an intact IgG1 molecule were shown to possess limited mobility. It was found that about 70°C of molecules in the IgG1 Van specimen are not flat but have a tripod...

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Veröffentlicht in:FEBS letters 1990-11, Vol.275 (1-2), p.221-225
Hauptverfasser: Ryazantsev, S.N., Abramov, V.M., Zav'yalov, V.P., Vasiliev, V.D.
Format: Artikel
Sprache:eng
Schlagworte:
Biological and medical sciences
Electron microscopy
Fundamental and applied biological sciences. Psychology
Humans
Immunoglobin G1
Immunoglobulin Fab Fragments - ultrastructure
Immunoglobulin G - ultrastructure
Microscopy, Electron
Molecular biophysics
Myeloma Proteins
Protein Conformation
Structure in molecular biology
Tridimensional structure
Tripod-like conformation
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Beschreibung
Zusammenfassung:Human immunoglobulin G1 Van was studied by negative staining, freeze drying and high resolution shadow casting. The Fab and Fe subunits of an intact IgG1 molecule were shown to possess limited mobility. It was found that about 70°C of molecules in the IgG1 Van specimen are not flat but have a tripod‐like shape.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(90)81476-5