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Cited by 1,989

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Molecular Weight Determination of Protein-Dodecyl Sulfate Complexes by Gel Electrophoresis in a Discontinuous Buffer System

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Neville, David M.·1971·Journal of Biological Chemistry

Abstract

This report describes methods and results obtained by combining the techniques of sodium dodecyl sulfate (SDS) gel electrophoresis and electrophoresis in discontinuous buffer systems. The SDS gel system utilizes a sulfate-borate discontinuity which stacks and unstacks protein-SDS complexes over a range of 2,300 to 320,000 daltons, providing high resolution fractionation. The properties of protein-SDS complexes are investigated by calculating retardation coefficients and apparent free mobilities from Ferguson plots. Apparent free mobilities are approximately constant, establishing a linear relationship between the logarithm of the relative mobility and the retardation coefficient. The retardation coefficient is shown both empirically and theoretically to be a uniform function of molecular weight of protein-SDS complexes over specified ranges, providing a rationale for determining molecular weight from plots of the negative logarithm of relative mobility against molecular weight.

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Metadata

Authors
Neville, D. M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1971-10
Volume
246
Issue
20
Pages
6328-6334
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1566240917
Cited by
1,989
References
1
FWCI
47.85
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Molecular Weight Determination of Protein-Dodecyl Sulfate Complexes by Gel Electrophoresis in a Discontinuous Buffer System. https://app.cochat.ai/papers/10.1016/s0021-9258(18)61792-2
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Neville, D. M. (1971). Molecular Weight Determination of Protein-Dodecyl Sulfate Complexes by Gel Electrophoresis in a Discontinuous Buffer System. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)61792-2

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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.