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The effect of calmodulin on the order of lipids in rhodopsin-free and rhodopsin-containing membranes has been studied using spin-label electron spin resonance methods. Calmodulin, up to 10(-6)M, did not change the measured order of lipids in bilayer membranes containing only rhodopsin. However, for bovine rod outer segment disc membranes, which contain rhodopsin and other proteins, calmodulin induced a significant concentration and temperature dependent increase in the order of the membrane lipids. This suggests that the site of calmodulin binding is remote from rhodopsin itself, and the nature of the binding appears to be a membrane surface phenomenon.

Type

Journal article

Journal

Biochem Biophys Res Commun

Publication Date

14/06/1985

Volume

129

Pages

517 - 521

Keywords

Animals, Binding Sites, Calmodulin, Cattle, In Vitro Techniques, Liposomes, Membrane Fluidity, Membranes, Photoreceptor Cells, Retinal Pigments, Rhodopsin, Rod Cell Outer Segment