TY - JOUR
T1 - Cryoprecipitogogue from normal serum
T2 - mechanism for cryoprecipitation of immune complexes.
AU - Hardin, J. A.
PY - 1981/7
Y1 - 1981/7
N2 - We designed this study to examine the relationship of cryoglobulins to immune complexes in sera of patients with rheumatic or infectious diseases. Polyethylene glycol was used to precipitate large proteins from normal serum and then was dialyzed away. The precipitated proteins were soluble in warm phosphate-buffered saline but at 4 degrees C they reversibly reprecipitated. As they reprecipitated, they selectively coprecipitated cold-soluble immune complexes. By NaDodSO4/polyacrylamide gel electrophoresis, these normal, nonimmunoglobulin cryoproteins were similar to the nonimmunoglobulin constituents of washed cryoimmunoglobulins from patients with rheumatic or infectious diseases. These findings suggest that cryoprecipitability is a property not of immune complexes themselves but of a group of large normal serum proteins. In inflammatory diseases, the concentrations of some of these proteins, responding as acute-phase reactants, may increase to the point where intermolecular attractive forces become prominent, particularly in the cold. Cold-augmented molecular aggregation between these nonimmunoglobulin proteins and immune complexes could then act to decrease their collective solubility and result in the cryoprecipitation of otherwise cold-soluble immune complexes.
AB - We designed this study to examine the relationship of cryoglobulins to immune complexes in sera of patients with rheumatic or infectious diseases. Polyethylene glycol was used to precipitate large proteins from normal serum and then was dialyzed away. The precipitated proteins were soluble in warm phosphate-buffered saline but at 4 degrees C they reversibly reprecipitated. As they reprecipitated, they selectively coprecipitated cold-soluble immune complexes. By NaDodSO4/polyacrylamide gel electrophoresis, these normal, nonimmunoglobulin cryoproteins were similar to the nonimmunoglobulin constituents of washed cryoimmunoglobulins from patients with rheumatic or infectious diseases. These findings suggest that cryoprecipitability is a property not of immune complexes themselves but of a group of large normal serum proteins. In inflammatory diseases, the concentrations of some of these proteins, responding as acute-phase reactants, may increase to the point where intermolecular attractive forces become prominent, particularly in the cold. Cold-augmented molecular aggregation between these nonimmunoglobulin proteins and immune complexes could then act to decrease their collective solubility and result in the cryoprecipitation of otherwise cold-soluble immune complexes.
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U2 - 10.1073/pnas.78.7.4562
DO - 10.1073/pnas.78.7.4562
M3 - Article
C2 - 6945599
AN - SCOPUS:0019590732
SN - 0027-8424
VL - 78
SP - 4562
EP - 4565
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 7
ER -