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Structural Studies on a Human IgAl Myeloma Protein with a Carboxy-Terminal Deletion¹

From the Division of Allergy and Clinical Immunology, Department of Medicine, National Jewish Hospital and Research Center, Denver, Colorado 80206, and the Children's Hospital, Columbus, Ohio 43205

Abstract

A human IgA1 monomeric myeloma protein (Vo) was found to be antigenically deficient to other IgA proteins. The molecular weight of the heavy chains was 42,000 daltons, compared with a figure of 58,000 daltons found for normal chains. In contrast, both the light (L) chains and the Fd' fragment had molecular weights identical to those of other IgAl proteins. Two cyanogen bromide fragments were isolated from the heavy (H) chains: one fragment consisted of the first 85 amino acid residues of the variable region, whereas the second one contained the remainder of the foreshortened chain. Neither the carboxy-terminal octapeptide of normal chains nor the cyanogen bromide fragment containing 30 amino acid residues and located in normal chains in a position preceding that of the octapeptide were found. The structural moiety missing in Vo and responsible for its antigenic deficiency was found to be a peptide consisting of more than 100 amino acid residues from the C-terminal end of the chain, probably involving the entire CH3 domain.

Footnotes

¹ This work was supported by United States Public Health Service, National Institutes of Health Grant AI-09758, Allergy Disease Center Grant AI-10398, GRS Grant RR 05504, and American Heart Association Grant 70–749.

² Supported by Fellowships from the Swiss Academy of Medical Sciences and the World Health Organization.

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