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An unusual case of a plasma cell neoplasm with an IgG3lambda myeloma and a gamma3 heavy chain disease protein

Adlersberg JB; Grann V; Zucker-Franklin D; Frangione B; Franklin EC
A unique case of gamma3 heavy chain disease with two related serum proteins is reported. One molecule appears to be an IgG3lambda myeloma protein. The second molecule is a dimer of a shortened gamma3 heavy chain that has an unblocked amino terminus and lacks the VH and CH1 domains. Its probable origin as a synthetic product is discussed. The clinical and pathologic features of this patient resemble those of other patients with gamma heavy chain disease more than those of patients with multiple myeloma. It seems likely that the heavy chain disease protein is the result of a mutational event in the malignant clone originally producing the myeloma protein.
PMID: 412532
ISSN: 0006-4971
CID: 9661

An antigenic determinant unique to the hinge of gamma3 heavy chains

Franklin EC; Frangione B; Adlersberg JB
PMID: 50356
ISSN: 0022-1767
CID: 9675

Repetitive hinge region sequences in human IgG3: isolation of an 11,000-dalton fragment

Adlersberg JB; Franklin EC; Frangione B
The heavy chain (gamma-3) of the IgG3 subclass of human immunoglobulins has a molecular weight of 60,000, instead of the 50,000 value reported for gamma-1, gamma-2, and gamma-4 heavy chains. By use of protein Omm, a gamma-3 heavy chain disease protein, it was possible to isolate and analyze the extra fragment. Protein Omm had a molecular weight of 40,000, glycine as its sole NH-2-terminal, and contained only the hingee region and the C-H-2 and C-H-3 domains. CNBr cleavage at Met 252 (gamma-1 numbering) yielded the hinge fraction (Fh fragment). On the basis of the molecular weight of Fh (11,000), its amino-acid composition, its partial sequence, and its unexpectedly low number of tryptic peptides, it is postulated that the extra fragment in gamma-3 heavy chains represents a series of similar or identical duplications of sections of the previously reported gamma-3 hinge region. In addition, there are striking homologies with the hinge region of alpha-1 and alpha-2 heavy chains, one of which also has duplications. The relationship of these hinge structures in different immunoglobulins supports the concept that this region is coded by a unique, small piece of DNA, which has evolved in parallel manner with the immunogolbulin genes by partial duplications and/or crossingover.
PMID: 804697
ISSN: 0027-8424
CID: 9677