SODIUM DODECYL SULFATE‐POLYACRYLAMIDE GEL ELECTROPHORESIS OF, CHROMATOGRAPHICALLY FRACTIONATED EGG WHITE

摘要

ABSTRACTAnalytical electrophoretic methods were used to observe heterogeneity in chromatographic isolates of native egg white proteins (NEW). NEW was fractionated by carboxymethylcellulose chromatography. Isolates were analyzed by polyacrylamide gel electrophoresis (PAGE) and sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE). Considerable heterogeneity was noted in several fractions thought previously to contain pure components. PAGE resulted in seven G, globulins eluted with ovalbumin A3. These uncharacterized globulins had molecular weights of 58,000. Several unknown components of large molecular weight (100,00–200,000) were eluted by alkaline buffers. Chromatography in conjunction with electrophoresis yielded several unidentified proteins requiring further characteriz