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Selective Solubilization of a Protein Component of the Red Cell Membrane
Abstract
Approximately 20 percent of the membrane-bound protein of erythrocyte ghosts can be solubilized and obtained free of other membrane components by dialysis against adenosine triphosphate and 2-mercaptoethanol. This protein forms one major band on polyacrylamide gels and a single boundary in free-boundary electrophoresis, and it undergoes polymerization in the presence of divalent cations to form coiled filaments visible by electron microscopy. Antibodies to this membrane protein react specifically with red blood cells or their membrane ghosts but do not react with serum, erythrocyte cytoplasm, or other blood cells. The functional role of this protein is unknown, but it appears to be involved in maintaining the structure of the red cell membrane. We suggest that this protein be called Spectrin since it is obtained from membrane ghosts.
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Citations
Cited by
Red cell membrane: past, present, and future
Mohandas, N., & Gallagher, P. G. (2008) · Blood · doi:10.1182/blood-2008-07-161166 · Cited by 1,089
Actin And Myosin And Cell Movemen
Pollard, T. D., Weihing, R. R., & Adelman, M. R. (1974) · CRC Critical Reviews in Biochemistry · doi:10.3109/10409237409105443 · Cited by 1,017
Transmembrane control of the receptors on normal and tumor cells
Nicolson, G. L. (1976) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(76)90014-9 · Cited by 959
Selective solubilization of proteins from red blood cell membranes by protein perturbants
Steck, T. L., & Yu, J. (1973) · Journal of Supramolecular Structure · doi:10.1002/jss.400010307 · Cited by 607
Staros, J. V. (1982) · Biochemistry · doi:10.1021/bi00260a008 · Cited by 485
Metadata
- Authors
- Marchesi, V. T., & Steers, E.
- Venue
- Science
- Published
- 1968-01-12
- Volume
- 159
- Issue
- 3811
- Pages
- 203-204
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1981906600
- Cited by
- 429
- References
- 0
- FWCI
- 35.49
- Type
- journal article
- Language
- en
- Open access
- closed
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