Abstract
Bovine as well as frog rod outer segments contain a membrane-bound protein which binds the GTP analog GppNp in the light (Kd=0.3μM). The amount of GppNp bound is 2.5–3.5 mmole per mol rhodopsin. The binding protein (M.Wt. ⋍ 54,000) can be extracted from rod membranes with detergent and purified on an Agarose column. The chromatographic profile indicates that the binding protein is distinct from rhodopsin, GTPase or cyclic nucleotide phosphodiesterase.
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