SUMMARY: Plasma membranes were isolated from the acellular slime mould by differential centrifugation and an aqueous two-phase polymer method. ATPase activity in the membrane fraction was optimal at pH 6.5 and was severely inhibited by vanadate but resistant to oligomycin. The protein components of the plasma membrane were analysed by polyacrylamide gel electrophoresis. Glycoproteins were located on Western blots by incubation of the sheets with lectin-peroxidase reagents. The results indicated that most of the membrane proteins were glycosylated. Pulse-chase experiments with [H]glucosamine showed that when the plasmodia were induced to differentiate to macrocysts, turnover of the membrane glycoproteins occurred more rapidly than in growing plasmodia.


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