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[Isolation of GTP-binding Gs-protein liberated from human erythrocyte membranes under the action of fluoride ions].

Human erythrocyte membranes were incubated in the presence of sodium fluoride. After centrifugation at 30,000 g for 30 min the supernatant was able to stimulate the catalytic subunit of adenylate cyclase. The stimulatory factor was purified from the supernatant of fluoride-treated membranes by three subsequent chromatographic steps including DEAE-Sephacel ion-exchange chromatography in the absence of detergent, gel-filtration on Ultrogel AcA 44 in the presence of 1% sodium cholate and phenyl-Sepharose CL/4B hydrophobic chromatography. The final preparation showed approximately 120-fold purification in stimulatory activity over the initial extract and contained two polypeptides (Mr 42 kDa and 36 kDa). The stimulator activity of the preparation was inhibited by 60% by beta gamma-subunits of the GTP-binding protein of bovine brain membranes, G0. The data obtained suggest that the regulatory GTP-binding stimulatory protein of adenylate cyclase, GS, dissociates from human erythrocyte membranes as a result of fluoride-ion treatment.