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Amino Acid Analysis of Serum Proteins in Multiple Myeloma^*

( Department of Physiological Chemistry, University of Wisconsin, Madison 6, Wis.)

Eight proteins have been separated by ammonium sulfate precipitation from the sera of different patients with multiple myeloma. The electrophoretic and ultracentrifugal properties of these proteins are summarized.

Analytical data for the amino acid composition of these proteins indicate differences among them, especially for one relatively insoluble protein which differed markedly from the rest in that it had an increased arginine and decreased tyrosine, leucine, and lysine concentrations. It was further distinguished by having as its main component a protein with a sedimentation constant (S) of 19.2. 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. The over-all similarity of the amino acid composition of these proteins to normal -globulin is discussed.

^* This investigation was supported in part by a research grant, C-822(C3) from the National Cancer Institute, of the National Institutes of Health, Public Health Service.

Received 5/28/53.

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