Abstract
MEMBRANE protein of bovine rod outer segments has been studied by gel electrophoresis and amino-acid analysis. Membranes were purified in a sucrose density gradient1 at an ionic strength below 0.001. The isolated material probably consisted of fragmented disk membranes1. ‘Emulphogene’ solutions of rhodopsin were chromatographed on calcium phosphate2; the results for A278: A498 were 1.7–1.8, indicating good purity.
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