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Related Experiment Videos

Heavy-chain variable regions in normal and pathological immunolobulins.

A C Wang, H H Fudenberg, J R Pink

    Proceedings of the National Academy of Sciences of the United States of America
    |June 1, 1971
    PubMed
    Summary

    Immunoglobulin G heavy chain analysis reveals VHIII subgroup sequences in all individuals, suggesting multiple genes, not alleles, form this region. A hypervariable sequence in VHIII is homologous to light chain regions.

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    Area of Science:

    • Immunogenetics
    • Molecular Biology
    • Protein Chemistry

    Background:

    • Immunoglobulin G (IgG) heavy chains possess variable regions crucial for antibody diversity.
    • The VHIII subgroup is a significant component of the human IgG heavy chain repertoire.

    Purpose of the Study:

    • To investigate the genetic basis of IgG heavy chain variable region subgroups.
    • To identify and characterize hypervariable regions within the VHIII subgroup.

    Main Methods:

    • Amino acid sequence analysis of immunoglobulin G heavy chains from 15 normal individuals.
    • N-terminal amino acid sequencing of ten myeloma protein heavy chains belonging to the VHIII subgroup.

    Main Results:

    • VHIII subgroup sequences were present in all 15 normal individuals, comprising 15-25% of total heavy chains.

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  • A hypervariable sequence region was identified between amino acid positions 30-35 in VHIII heavy chains, homologous to light chain hypervariable regions.
  • Sequence variants within the VHIII subgroup suggest origins from multiple, recently evolved genes.

    • Conclusions:

    • The diverse subgroups of the immunoglobulin heavy-chain variable region are likely encoded by multiple genes, not allelic variants of a single gene.
    • The identified hypervariable region in VHIII contributes to antibody diversity and shares homology with light chain structures.