Complete covalent structure of a human IgA1 immunoglobulin

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

doi:10.1126/science.821146

Complete covalent structure of a human IgA1 immunoglobulin

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

Research output: Contribution to journal › Article › peer-review

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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 language	English (US)
Pages (from-to)	1017-1020
Number of pages	4
Journal	Science
Volume	193
Issue number	4257
DOIs	https://doi.org/10.1126/science.821146
State	Published - 1976
Externally published	Yes

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title = "Complete covalent structure of a human IgA1 immunoglobulin",

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.",

author = "Liu, {Yu Sheng Victor} and Low, {Teresa L.K.} and Anthony Infante and Putnam, {Frank W.}",

year = "1976",

doi = "10.1126/science.821146",

language = "English (US)",

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AU - Low, Teresa L.K.

AU - Infante, Anthony

AU - Putnam, Frank W.

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N2 - 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.

AB - 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.

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Complete covalent structure of a human IgA1 immunoglobulin

Abstract

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