A study of serum protein fractionation.
Serum protein fractionation was studied using the techniques of ammonium sulfate precipitation, molecular seiving chromatography, and ion-exchange chromatography. Whole human serum was fractionated by precipitation with ammonium sulfate at 40, 50, 60, and 70 percent saturation. Molecular seiving chromatography was performed on whole human serum and on four ammonium sulfate precipitated fractions. The eluted peaks from molecular seiving chromatography were further separated by ion-exchange chromatography to obtain isolated fractions of IgG, transferrin, and albumin. Qualitative analysis of the various fractions and assessment of the purity of isolated IgG, transferrin, and albumin was done by polyacrylamide gel electrophoresis and by immunoelectrophoresis.
D000645:Ammonium Sulfate; D001798:Blood Proteins / Q000032:analysis*; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007122:Immunoelectrophoresis; D007074:Immunoglobulin G / Q000032:analysis; D012709:Serum Albumin / Q000032:analysis; D014168:Transferrin / Q000032:analysis
D001798:Blood Proteins; D007074:Immunoglobulin G; D012709:Serum Albumin; D014168:Transferrin; D000645:Ammonium Sulfate