PMID: 6781064Jan 1, 1980Paper

Structural studies of three IgG kappa proteins from a patient with multiple myeloma

Scandinavian Journal of Immunology
E DworskyP Wetteland

Abstract

Three distinct IgG proteins of similar concentration and the same light-chain type were demonstrated in a myeloma serum. The bonds between the heavy and light chains were split, and the isolated gamma- and kappa-chains were characterized by crossed immunoelectrophoresis, subgroup determination and N-terminal amino acid sequence. The studies showed that the IgG heterogeneity was due to differences in the primary structure of the variable parts of the kappa-chains. Two of the kappa-chains belonged to subgroup V kappa I, and one chain, the most anodic one, belonged to V kappa III The gamma-chains were homogeneous and belonged to subgroup VHIII.

References

Jan 1, 1976·Scandinavian Journal of Immunology·J B NatvigT E Michaelsen
Jan 1, 1972·Scandinavian Journal of Immunology·M HarboeK Sletten
Jul 1, 1969·The American Journal of Medicine·J H SandersC Berard
Jan 1, 1972·Methods in Enzymology·W Konigsberg

Related Concepts

Molecular Sieve Chromatography
Polyglobin
Immunoelectrophoresis, Two-Dimensional
Gamma-2b-Immunoglobulin Heavy Chain
Kappa-Immunoglobulin Subgroup VK-21
Immunoglobulin Light Chains
Multiple Myeloma

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