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Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium
Authors:D Emeis  H Kühn  J Reichert  K P Hofmann
Institution:1. Department of Biochemistry, Bowman Gray School of Medicine, Winston-Salem, NC 27103, USA;2. Department of Medicine, Bowman Gray School of Medicine, Winston-Salem, NC 27103, USA;3. Department of Medicinal Chemistry, School of Pharmacy, University of North Carolina, Chapel Hill, NC 27514, USA
Abstract:Cap binding protein (CBP)-related polypeptides were identified in different cytoplasmic RNP particles of embryonic chick muscles using monoclonal antibody to purified CBP. A single immunoreactive peptide (Mr 78000) was present in preparations of both free mRNP particles and a novel 10 S translation inhibitory RNP particle. In contrast, proteins isolated from these particles showed two new low-Mr immunoreactive peptides (Mr 43000 and Mr 29000). No CBP related protein could be detected in polysomal mRNP, although an immunoreactive Mr 43000 CBP-related protein was present in polysomes. The relevance of the association of different CBP-related polypeptides with cytoplasmic RNP particles and polysomes are discussed.
Keywords:ROS  rod outer segments  G-protein  GTP-binding protein  MI  metarhodopsin I  MII  metarhodopsin II  GTP-γS  NIR  near-infrared
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