The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
The Gross Conformation of Protein-Sodium Dodecyl Sulfate Complexes
Open accessAbstract
Abstract The interaction of sodium dodecyl sulfate with a wide variety of proteins is characterized by a high binding ratio when the monomer concentration of amphiphile exceeds 5 x 10-4 m. This binding ratio on a gram to gram basis is identical for all proteins investigated. The protein portion of the complex contains a high degree of order, and hydrodynamic studies suggest that the complex is a rodlike particle, the length of which varies uniquely with the molecular weight of the protein moiety. These results explain the empirical observation that proteins dissolved in aqueous solutions containing high concentrations of sodium dodecyl sulfate have electrophoretic mobilities on polyacrylamide gels which are a unique function of their molecular weights. In addition, the data suggest a possible model for the conformation of membrane proteins and their interactions with phospholipid.
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Cites
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
Dodge, J. T., Mitchell, C., & Hanahan, D. J. (1963) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(63)90042-0 · Cited by 4,393
Physical chemistry of macromolecules
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Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels
Shapiro, A. L., Viñuela, E., & V. Maizel, J. (1967) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(67)90391-9 · Cited by 3,763
Tanford, C. (1968) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60401-5 · Cited by 2,130
Self-citationPhysical chemistry of macromolecules
Fixman, M. (1962) · Comparative Biochemistry and Physiology · doi:10.1016/0010-406x(62)90048-8 · Cited by 2,017
Reynolds, J. A., & Tanford, C. (1970) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.66.3.1002 · Cited by 695
Self-citationA Simple Chromatographic Method for Preparation of Gamma Globulin.
Levy, H. B., & Sober, H. A. (1960) · Experimental Biology and Medicine · doi:10.3181/00379727-103-25476 · Cited by 617
The native, denatured and renatured states of deoxyribonucleic acid
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Multiple Equilibria in Proteins
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Cited by
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
Self-citationProtein blotting: Principles and applications
Gershoni, J. M., & Palade, G. E. (1983) · Analytical Biochemistry · doi:10.1016/0003-2697(83)90128-8 · Cited by 853
Covalent lipoprotein from the outer membrane of Escherichia coli
Braun, V. (1975) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(75)90013-1 · Cited by 580
Proteomics of Integral Membrane ProteinsTheory and Application
Speers, A. E., & Wu, C. C. (2007) · Chemical Reviews · doi:10.1021/cr068286z · Cited by 325
Structure and function of the epidermal barrier
Wickett, R. R., & Visscher, M. O. (2006) · American Journal of Infection Control · doi:10.1016/j.ajic.2006.05.295 · Cited by 327
Metadata
- Authors
- Reynolds, J. A., & Tanford, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1970-10
- Volume
- 245
- Issue
- 19
- Pages
- 5161-5165
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1486292873
- Cited by
- 938
- References
- 13
- FWCI
- 99.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
