Abstract
IT has recently been shown in several laboratories that if isolated rod outer segments (ROS) are incubated in the presence of MgATP, rhodopsin is phosphorylated (see ref. 1). The reaction is much faster after the ROS have been exposed to light as the enzyme, ‘opsin kinase’, is specific to bleached rather than unbleached rhodopsin1. It has been suggested that the function of rhodopsin phosphorylation may be to regulate the responsiveness of ROS to light and in this paper we describe a mechanism whereby such a regulation could occur.
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