Complete covalent structure of a human IgA1 immunoglobulin

Yu Sheng Victor Liu, Teresa L.K. Low, Anthony Infante, Frank W. Putnam

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Abstract

The complete covalent structure has been determined for a human myeloma IgA1 immunoglobulin. This protein has unique features in the amino acid sequence and disulfide bridge structure of the variable (V) and constant (C) regions of both the α heavy and the λ light chains, and in the number and loci of oligosaccharides. Whereas C region domains of heavy chains have evolved independently over eons, recent isotypic variations have occurred in λ light chains and possibly in a heavy chains.

Original languageEnglish (US)
Pages (from-to)1017-1020
Number of pages4
JournalScience
Volume193
Issue number4257
DOIs
StatePublished - Jan 1 1976
Externally publishedYes

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Cite this

Liu, Y. S. V., Low, T. L. K., Infante, A., & Putnam, F. W. (1976). Complete covalent structure of a human IgA1 immunoglobulin. Science, 193(4257), 1017-1020. https://doi.org/10.1126/science.821146