The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Selective solubilization of proteins from red blood cell membranes by protein perturbants
Abstract
Isolated human erythrocyte membranes were exposed to a series of reagents known to modify or perturb proteins; these included sodium hydroxide, lithium diiodosalicylate, acid anhydrides, and organic mercurials. Each reagent liberated the same set of relatively polar polypeptides from the membrane, while the other, more hydrophobic species invariably remained associated with the membrane residue. The selective elution pattern was precisely that seen previously with 6 M guanidine hydrocloride. The released polypeptides, comprising half of the membrane protein mass, contained no carbohydrate; current evidence indicates that all of these components are confined to the cytoplasmic surface of the membrane. The residue contained all the lipids and all the glycoproteins. The latter are accessible to the outer membrane surface and, in at least two cases, seem to extend asymmetrically across the thickness of the membrane. Thus, the distinctive elution behavior which defines these two groups of polypeptides relates both to their chemical composition and their organizational disposition in the membrane.
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Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
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A SIMPLE METHOD FOR THE ISOLATION AND PURIFICATION OF TOTAL LIPIDES FROM ANIMAL TISSUES
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Colorimetric Method for Determination of Sugars and Related Substances
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Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
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Self-citationThe Thiobarbituric Acid Assay of Sialic Acids
Warren, L. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)69851-5 · Cited by 6,433
[10] Assay of inorganic phosphate, total phosphate and phosphatases
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Tanford, C. (1970) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60241-7 · Cited by 1,277
Yu, J., Fischman, D. A., & Steck, T. L. (1973) · Journal of Supramolecular Structure · doi:10.1002/jss.400010308 · Cited by 697
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Cited by
Fujiki, Y., Hubbard, A. L., Fowler, S., & Lazarow, P. B. (1982) · The Journal of cell biology · doi:10.1083/jcb.93.1.97 · Cited by 1,751
Characterization of membrane proteins in detergent solutions
Tanford, C., & Reynolds, J. A. (1976) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(76)90009-5 · Cited by 854
Yu, J., Fischman, D. A., & Steck, T. L. (1973) · Journal of Supramolecular Structure · doi:10.1002/jss.400010308 · Cited by 697
Self-citationMonoclonal antibodies identify a group of nuclear pore complex glycoproteins.
Snow, C. M., Senior, A., & Gerace, L. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.5.1143 · Cited by 538
Jay, S. D., Sharp, A. H., Kahl, S. D., Vedvick, T. S., Harpold, M. M., & Campbell, K. P. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)49986-3 · Cited by 259
Metadata
- Authors
- Steck, T. L., & Yu, J.
- Venue
- Journal of Supramolecular Structure
- Publisher
- Wiley
- Published
- 1973-01
- Volume
- 1
- Issue
- 3
- Pages
- 220-232
- ISSN
- 0091-7419 (ISSN-L)
- 1547-9366
- OpenAlex
- W1968745789
- Cited by
- 607
- References
- 21
- FWCI
- 10.75
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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