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1. Two membrane fractions were separated from rabbit white muscle SR by discontinuous sucrose gradient. 2. Both crude and membrane fractions were shown to contain AChE, Ca2+-stimulated and Ca2+- independent ATPase activities. 3. 1% W/V Triton X-100 solubilized most of the AChE and Ca2+-stimulated ATPase but the Ca2+- independent ATPase was poorly solubilized. 4. AChE was sensitive to BW284c51, non-sensitive to ethopropazine and presented inhibition by excess of the substrate, ATCh. 5. Polyacrylamide gel electrophoresis from Triton-treated crude SR revealed several bands of AChE and ATPase activities. 6. SDS-gel electrophoresis from crude SR showed two polypeptides specifically labelled with [3H]DFP.
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