Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.

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...

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Main Authors: Volotovski, I, Ryba, N, Watts, A
Format: Journal article
Language:English
Published: 1985
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author Volotovski, I
Ryba, N
Watts, A
author_facet Volotovski, I
Ryba, N
Watts, A
author_sort Volotovski, I
collection OXFORD
description 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.
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spelling oxford-uuid:606f9dba-1a23-4313-8abb-a6589c47405d2022-03-26T17:53:30ZEffect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:606f9dba-1a23-4313-8abb-a6589c47405dEnglishSymplectic Elements at Oxford1985Volotovski, IRyba, NWatts, AThe 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.
spellingShingle Volotovski, I
Ryba, N
Watts, A
Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.
title Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.
title_full Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.
title_fullStr Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.
title_full_unstemmed Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.
title_short Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.
title_sort effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin containing phospholipid vesicles
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AT ryban effectofcalmodulinonthestructuralstateofphotoreceptormembranesandrhodopsincontainingphospholipidvesicles
AT wattsa effectofcalmodulinonthestructuralstateofphotoreceptormembranesandrhodopsincontainingphospholipidvesicles