sodium-dodecyl-sulfate and Waldenstrom-Macroglobulinemia

High resolution two-dimensional (2D)-electrophoresis has been developed to the stage that it is possible to resolve several thousand proteins in cells and tissue, and over six-hundred proteins are separated in human serum. The 2D-technique has been applied to analyses of serum from patients with multiple myeloma, macroglobulinemia and other gammopathies, and to separate apolipoproteins and study abnormalities and polymorphism of these proteins. Cerebrospinal fluid from patients with various neurological diseases has been studied by 2D-electrophoresis and seems to yield information on multiple sclerosis. The 2D-technique has been applied to normal and malignant cells and biopsies, and offers a possibility to detect disease-related proteins. Protein spots from 2D-gels may be used to raise monoclonal antibodies which subsequently can be used to develop simple clinical chemical tests for disease markers. The 2D-electrophoretic method is, however, not yet suitable as a typical routine analysis in the clinical chemistry laboratory, but is primarily a research tool of considerable potential.

Topics: Blood Proteins; Cerebrospinal Fluid Proteins; Electrophoresis, Polyacrylamide Gel; Humans; Hypergammaglobulinemia; Isoelectric Focusing; Multiple Myeloma; Nervous System Diseases; Proteins; Sodium Dodecyl Sulfate; Waldenstrom Macroglobulinemia

Sera from normal persons and patients with IgA, IgD, IgG, and IgM monoclonal gammopathies were electrophoresed in polyacrylamide gels containing sodium dodecyl sulfate. The gels were stained with Coomassie blue or were used for immunodiffusion. By this method IgG multiple myeloma and IgM Waldenström's macroglobulinemia sera were readily distinguished by electrophoresis alone, whereas IgA and IgD myeloma sera were distinguished by further immunodiffusion against anti-alpha-chain antibody and anti-delta-chain antibody.

Topics: Electrophoresis, Polyacrylamide Gel; Humans; Immunodiffusion; Immunoglobulin A; Immunoglobulin D; Immunoglobulin G; Immunoglobulin M; Immunoglobulins; Multiple Myeloma; Sodium Dodecyl Sulfate; Waldenstrom Macroglobulinemia

J chain was isolated from sulphonated human immunoglobulin M molecules by electrophoresis on polyacrylamide gels. When determined by electrophoresis in sodium dodecyl sulphate-polyacrylamide gels, the molecular weight of the protein was about 27000. After suspension in 5m-guanidine hydrochloride solution for 21 days, two groups of three bands appeared on the gels. Most of the protein dissociated to components of molecular weight 15000. The molecular weight of purified J chain was also determined by ultracentrifugation. In borate-saline solution the average weight-average molecular weight was about 29000. The molecular weight slowly decreased upon prolonged exposure to guanidine hydrochloride, and after 14 days the minimum molecular weight was about 15000. Some association between chains still existed. These data suggest that J chain derived from the paraprotein exists in borate-saline solution as dimers held by strong non-covalent forces.

Topics: Chromatography, Gel; Electrophoresis, Polyacrylamide Gel; Guanidines; Humans; Hydrogen-Ion Concentration; Immunodiffusion; Immunoelectrophoresis; Immunoglobulin J-Chains; Immunoglobulin M; Macromolecular Substances; Molecular Weight; Protein Binding; Protein Conformation; Sodium Dodecyl Sulfate; Spectrophotometry, Ultraviolet; Time Factors; Ultracentrifugation; Waldenstrom Macroglobulinemia

Topics: Chemical Phenomena; Chemistry; Dialysis; Electrophoresis, Polyacrylamide Gel; Guanidines; Humans; Immunoglobulin J-Chains; Immunoglobulin M; Molecular Weight; Polymers; Protein Conformation; Sodium Dodecyl Sulfate; Waldenstrom Macroglobulinemia

Topics: Acetates; Acrylamides; Blood Proteins; Electrophoresis, Disc; Humans; Methods; Proteins; Rosaniline Dyes; Sodium Dodecyl Sulfate; Staining and Labeling; Time Factors; Waldenstrom Macroglobulinemia