Thermodynamic basis for the abnormal solubility of monoclonal cryoimmunoglobulins.
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.
D000818:Animals; D002417:Cattle; D003450:Cryoglobulins; D005634:Fructose-Bisphosphate Aldolase; D006441:Hemoglobin A; D006451:Hemoglobin, Sickle; D006801:Humans; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D010108:Oxyhemoglobins; D011092:Polyethylene Glycols; D011817:Rabbits; D012710:Serum Albumin, Bovine; D012995:Solubility; D013816:Thermodynamics
D003450:Cryoglobulins; D006451:Hemoglobin, Sickle; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D010108:Oxyhemoglobins; D012710:Serum Albumin, Bovine; D011092:Polyethylene Glycols; D006441:Hemoglobin A; D005634:Fructose-Bisphosphate Aldolase