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Heterogeneity in the conformation of different protein fractions from the human erythrocyte membrane

✍ Scribed by Holzwarth, G. ;Yu, John ;Steck, Theodore L.


Publisher
Wiley (John Wiley & Sons)
Year
1976
Tongue
English
Weight
437 KB
Volume
4
Category
Article
ISSN
0091-7419

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✦ Synopsis


Abstract

We have isolated 5 families of proteins from human red blood cell membranes and characterized their secondary structure by ultraviolet circular dichroism measurements. The protein families were prepared by selective solubilization from ghosts under nondenaturing conditions. We find that the intact ghost has a mean α‐helix fraction of 0.37, whereas a low‐ionic‐strength extract (bands 1, 2, 5, β€œspectrin”) has a substantially higher helix fraction, 0.55. Further extraction of the ghosts with para‐chloromercuribenzoate yields bands 2.1, 4.1, 4.2, and 6; their helix content is only 0.17. Finally, the major intrinsic protein, band 3, was solubilized by a nonionic detergent. Its helix fraction is 0.38.


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