Abstract
The treatment of red blood cell membranes with 6 M guanidine hydrochloride plus reduction and alkylation produces a turbid suspension which is resolved by ultracentrifugation into a clear solution and an overlying membraneous pelliccle. As analyzed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, the guanidine·HCl-soluble fraction is deficient in a major polypeptide component (III), the principal sialoglycoproteins, and some minor bands, all of which are selectively concentrated in the buoyant lipoid layer. These data suggest the particular lipophilicity of these unsolubilized polypeptides and account for the discrepancy between preparations of membrane proteins solubilized in sodium dodecyl sulfate and in guanidine·HCl.
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