Biosynthetic And structural studies of a heavy chain disease protein

Daniel Ein; Donald N. Buell; John L. Fahey

doi:10.1172/JCI106036

¹Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014

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¹Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014

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¹Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014

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Published in Volume 48, Issue 4 on April 1, 1969
J Clin Invest. 1969;48(4):785–793. https://doi.org/10.1172/JCI106036.
© 1969 The American Society for Clinical Investigation

Published April 1, 1969 - Version history

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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