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Abstract
Highly purified bovine retinal outer segments are isolated by centrifugation. Localization of ATPase is studied with three preparations including intact, shocked (1 min in water), and lysed (10 min in water) outer segments. The activity of Mg 2+-ATPase is equally high in these preparations. Na +, K +-activated ATPase is negligible in intact outer segments but is about 10-fold higher in the shocked and lysed preparation. K +-stimulated phosphatase shows a similar distribution except that the activity is higher in lysed outer segments as compared to the shocked ones. These data indicate that the discs contain a Na +, K +-activated ATPase with the ATP site on their external surface. ATP-binding assays also support the interpretation. The enzyme would accumulate Na + ions into the discs and transport K + ions out of them.
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