## Abstract Component a of the erythrocyte membrane is a specific substrate for endogenous protein kinase activity and its phosphorylation is significantly decreased under assay conditions in myotonic muscular dystrophy (Roses, A. D., and Appel, S. H., J. Membr. Biol. 20:51β58 (1975)). We have demo
Heterogeneity in the conformation of different protein fractions from the human erythrocyte membrane
β 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
No coin nor oath required. For personal study only.
β¦ 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 Ξ±βhelix fraction of 0.37, whereas a lowβionicβstrength extract (bands 1, 2, 5, βspectrinβ) has a substantially higher helix fraction, 0.55. Further extraction of the ghosts with paraβchloromercuribenzoate 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.
π SIMILAR VOLUMES
To reveal the role of the band 3 anion transport protein of the erythrocyte membrane in drug transport through the membrane, the possible effects of inhibitors of anion transport on the permeability of some anionic drugs were examined. The amounts of these drugs that permeated varied markedly with t