Structure of human myeloma IgG3 Kuc

Eur J Biochem. 1990 Jun 20;190(2):393-9. doi: 10.1111/j.1432-1033.1990.tb15588.x.

Abstract

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 degrees C or pH 7.8, 65 degrees C) lead to 'unfolding' of the hinge region which has a rod-like shape in electron micrographs.

MeSH terms

  • Freeze Drying
  • Humans
  • Hydrogen-Ion Concentration
  • Immunoglobulin G / isolation & purification
  • Immunoglobulin G / ultrastructure*
  • Immunoglobulin Variable Region / physiology
  • Microscopy, Electron
  • Multiple Myeloma / immunology*
  • Protein Conformation
  • Protein Denaturation
  • Staining and Labeling
  • Temperature
  • Ultracentrifugation

Substances

  • Immunoglobulin G
  • Immunoglobulin Variable Region