Abstract
Summary
Polyacrylamide gel electrophoresis in DS revealed certain similarities in the patterns for protein components of solubilized erythrocyte membranes and their cytoplasmic washings. Gels run without the addition of DS also showed similarities for membrane components and cytoplasmic washings, but they differed markedly from those obtained with DS-electrophoresis. Identical observations were made with bovine, equine, human and rabbit erythrocytes.
Electrophoretic patterns of erythrocyte constituents run in the presence of DS were similar for all four species, but in the absence of this anionic detergent standard-gel patterns of proteins showed considerable interspecies variation.
Proteins solubilized from ghosts by extraction with DS, butanol, pyridine, water, EDTA or TX had similar mobilities when electrophoresis was conducted in the presence of DS. The absence of DS during electrophoresis permitted many of the membrane constituents solubilized by these different procedures to form aggregates and migrate as diffuse bands, rendering their comparison difficult.
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