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. 1974 Apr;71(4):1123–1127. doi: 10.1073/pnas.71.4.1123

Amino-Acid Sequence of the Variable Region of the Heavy (Alpha) Chain of a Mouse Myeloma Protein with Anti-Hapten Activity

Sharron H Francis *,*, R Graham Q Leslie *,†, Leroy Hood ‡, Herman N Eisen *,§
PMCID: PMC388175  PMID: 4524622

Abstract

Cyanogen bromide cleavage of the heavy (alpha) chain of protein 315 (an immunoglobulin A mouse myeloma protein with anti-dinitrophenyl activity) yielded five fragments of which one (CN2), with 156 residues, contained the chain's entire variable region. Determination of the amino-acid sequence of CN2 showed that: (1) the variable region has appreciable homology (about 33% identities) with the variable region of the light chain from the same molecule; and (2) the constant-region sequence immediately following the probable transition from variable to constant domains is the same in the protein-315 α as in human γ1 and μ chains (-Val-Ser-Ser-). The sequence of the cyanogen bromide octapeptide (CN5) from the carboxy terminus of the protein-315 heavy chain closely resembles the corresponding segments of human α and μ chains.

Keywords: CNBr cleavage, alpha immunoglobulin chains, anti-dinitrophenyl activity

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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