PMID: 6410498Aug 1, 1983Paper

Biochemical and biosynthetic studies of a crystallizable human gamma 1 heavy-chain disease protein

Scandinavian Journal of Immunology
E MihaescoC Mihaesco

Abstract

We have studied the structure of a crystallizable gamma 1 heavy-chain disease protein that lacks the entire VH and C gamma 1 domains. The protein starts within the hinge region at aspartic acid 221 (Eu numbering). The native protein is a disulphide-linked dimer with an apparent molecular weight of 52,000, consistent with the biochemical data obtained on the whole protein and its cyanogen bromide fragments. The carbohydrate content of this protein was 6.8%. As shown by biosynthesis experiments intracytoplasmic gamma chains synthesized by neoplastic cells had an apparent molecular weight similar to that of the serum heavy-chain disease protein. These data are compared with those obtained for other gamma 1 heavy-chain disease proteins beginning in the hinge region, and the mechanisms leading to those abnormal Ig products are discussed.

References

Mar 1, 1978·European Journal of Immunology·S L Morrison
Jan 1, 1979·Immunological Reviews·M SeligmannJ C Brouet
Jan 11, 1969·Nature·B FrangioneE C Franklin
Dec 31, 1971·Annals of the New York Academy of Sciences·W D Terry, D Ein
Nov 1, 1981·Proceedings of the National Academy of Sciences of the United States of America·W Dackowski, S L Morrison
Oct 1, 1980·European Journal of Biochemistry·E MihaescoN Hilschmann
Jan 1, 1980·Scandinavian Journal of Immunology·J BiewengaE van Loghem
Jan 1, 1981·Scandinavian Journal of Immunology·P Guglielmi, J L Preud'homme
May 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·A AlexanderJ N Buxbaum
Sep 1, 1964·The American Journal of Medicine·E C FRANKLINM MELTZER

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Citations

Jan 1, 1991·Journal of Clinical Laboratory Analysis·P AucouturierJ L Preud'homme
May 1, 1987·Molecular Immunology·P AucouturierJ L Preud'homme
Apr 15, 1987·Klinische Wochenschrift·W StühlingerD Pastner

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