Rotational diffusion of erythrocyte membrane proteins

Cherry, R. J. and Nigg, E. A.. (1981) Rotational diffusion of erythrocyte membrane proteins. Progress in clinical and biological research, Vol. 51. pp. 59-77.

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Official URL: http://edoc.unibas.ch/dok/A5249527

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Rotational diffusion of band 3 proteins in human erythrocyte membranes is measured by observing flash-induced transient dichroism of the triplet probe, eosin-maleimide. At physiological temperature, both fast and slowly rotating populations of band 3 are present in the membrane. Rotational motion of band 3 is the same in membranes from young and old erythrocytes and is unchanged when the cholesterol:phospholipid mole ratio is varied from 1.34 to 1.66. Antibodies against glycophorin A immobilize band 3, indicating an association between these two integral membrane proteins. However, glycophorin A has little effect on the rotational motion of the complex, since band 3 rotation in En(a-) membranes (which lack glycophorin A) is similar to that observed in normal membranes. Cleavage of the cytoplasmic segment of band 3 by trypsin produces a considerable enhancement of band 3 rotational mobility. A similar effect is seen following extraction of bands 2.1 and 4.1 by sequential low salt-high salt treatment. It is concluded that up to 40% of band 3 has restricted rotational mobility due to interaction with the erythrocyte cytoskeleton.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum
05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Cell Biology (Nigg)
UniBasel Contributors:Nigg, Erich A.
Item Type:Article, refereed
Article Subtype:Research Article
Note:Also published in: The function of red blood cells. - New York : A.R. Liss, 1981. - S. 59-77 -- Publication type according to Uni Basel Research Database: Journal article
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Last Modified:22 Mar 2012 14:27
Deposited On:22 Mar 2012 13:59

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