Turnover of labeled normal gamma globulin in multiple myeloma.

@article{Lippincott1960TurnoverOL,
  title={Turnover of labeled normal gamma globulin in multiple myeloma.},
  author={Stuart W. Lippincott and Samuel Korman and Conrad T. O. Fong and E. E. Stickley and William Wolins and Walter L. Hughes},
  journal={The Journal of clinical investigation},
  year={1960},
  volume={39},
  pages={
          565-72
        },
  url={https://api.semanticscholar.org/CorpusID:8021497}
}
The approach to the investigation of certain fundamental aspects of protein metabolism in this disease has been concerned with the patient's turnover of globulins, and the biological half-life of gamma globulin fractionated from normal individuals, labeled with I131 and injected into ten patients with clinically proven multiple myeloma is presented.
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15 References

A new concept of the metabolism of the pathological proteins in myelomatosis.

The principal features of myelomatosis are the presence of abnormal globulins in the blood and of pathological cells resembling plasma cells in the bone marrow and in one experiment there is suggestion that, in the disease, the liver may be involved in the synthesis of these abnormal Globulins.

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It is suggested that most multiple myeloma proteins fall into two groups or families of cross-reacting abnormal proteins, one closely related to normal γ-globulin, the other distantly related toγ- globulin with marked individual specificities.

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In a comparison with the amino acid composition of normal gamma globulins, the myeloma proteins were in general high in lysine and proline and low in valine and the over-all similarity of the amino acids composition of these proteins to normal γ-globulin is discussed.

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