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J. Biol. Chem., Vol. 255, Issue 14, 6532-6534, 07, 1980

Thermodynamic basis for the abnormal solubility of monoclonal cryoimmunoglobulins

CR Middaugh, EQ Lawson, GW Litman, WA Tisel, DA Mood and A Rosenberg

The thermodynamics of both normal and abnormal (disease-associated) protein solubility has been examined. It is shown that the atypical behavior of monoclonal cryoimmunoglobulins can be explained by the formation of one or a few additional electrostatic contacts or, less frequently, a larger number of van der Waals interactions in the protein-rich solid phase relative to normal immunoglobulin. It is hypothesized that cryoimmunoglobulins represent the outer edge of the solubility distribution of total serum immunoglobulin.
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