Abstract
The mobility of benzyl alcohol molecules in erythrocyte membranes has been measured by nuclear magnetic resonance relaxation. At low concentrations the alcohol molecules are strongly immobilized by the membrane structure, this decreases as the concentration rises but starts to increase again at 60 mM. Suspensions of membrane lipid produce similar effects on relaxation at low concentrations but show no upswing at high concentrations. Separated membrane protein has a large effect on benzyl alcohol relaxation rate as have erythrocyte membranes pretreated with 300 mM benzyl alcohol.
These results suggest that as a result of insertion of time anesthetic in the membrane the lipid becomes disordered and finally exposes the protein, making available binding sites in the protein which are occult in the untreated membrane.
ACKNOWLEDGMENTS We are most grateful to Dr. J. Feeney and Varian Associates for their generosity in allowing us to make extensive use of an A-60A spectrometer. We are also grateful to the Smith, Kline and French Foundation for a grant in aid and to Miss Janet Swales for excellent assistance.
- Copyright ©, 1968, by Academic Press Inc.
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