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. 1969 Apr;48(4):785–793. doi: 10.1172/JCI106036

Biosynthetic And structural studies of a heavy chain disease protein

Daniel Ein 1, Donald N Buell 1, John L Fahey 1
PMCID: PMC322283  PMID: 4180120

Abstract

A new heavy chain disease protein (γHCD-JM) has been characterized by antigenic and structural criteria. The protein belongs to the IgG3-subclass and is closely related to Fc-fragment of G3-immunoglobulins. The predominant N-terminal amino acid of this protein is glutamic acid in the uncyclized form, and that of another γHCD is glycine.

Studies of the N-terminal peptides indicate that the N-terminal portion of the γ3-heavy polypeptide chain is absent from the γHCD-JM. These findings rule out a process of normal heavy chain initiation and a large deletion of the Fd region as being responsible for these two heavy chain disease proteins.

The γHCD-JM is a secretory product of cells from bone marrow as shown by studies of in vitro incorporation of amino acids-14C. Bone marrow and lymph node have a population of lymphoplasmacytic cells which by immunofluorescence contain γ-heavy chain antigens in the absence of light chain antigens.

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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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