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Isolation, Properties, and Structure of Human IgA Myeloma Globulins

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The Immunoglobulin a System

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Abstract

For the past few years our work has been based on the principle that the characteristic covalent structure of 99% of all human immunoglobulins could be established by determining the amino acid sequence of five kinds of polypeptide chains: κ and λ light chains, and γ, μ, and a heavy chains. We reported the first complete sequence of κ (1) and λ (2,3) light chains. Others sequenced the γ chain (4,5) and we recently reported the complete sequence of the μ chain (6). The a chain is the last of the big five, and many laboratories are now engaged in its study.

Supported by NIH CA08497, the Damon Runyon Fund (DRG-1134), and the American Cancer Society (NP-10).

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Author information

Authors and Affiliations

  1. Department of Zoology, Indiana University, Bloomington, 47401, Indiana, USA

    Frank W. Putnam, Teresa Low, Victor Liu, Hans Huser, E. Raff, F. C. Wong & J. R. Clamp

Authors
  1. Frank W. Putnam
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  2. Teresa Low
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  3. Victor Liu
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  4. Hans Huser
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  5. E. Raff
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  6. F. C. Wong
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  7. J. R. Clamp
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Editor information

Editors and Affiliations

  1. Institute of Dental Research Departments of Microbiology and Medicine, University of Alabama in Birmingham, Birmingham, Alabama, USA

    Jiri Mestecky

  2. Departments of Pediatrics and Microbiology, University of Alabama in Birmingham, Birmingham, Alabama, USA

    Alexander R. Lawton

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© 1974 Plenum Press, New York

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Putnam, F.W. et al. (1974). Isolation, Properties, and Structure of Human IgA Myeloma Globulins. In: Mestecky, J., Lawton, A.R. (eds) The Immunoglobulin a System. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-4550-3_20

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  • DOI: https://doi.org/10.1007/978-1-4613-4550-3_20

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-4552-7

  • Online ISBN: 978-1-4613-4550-3

  • eBook Packages: Springer Book Archive

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