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Cited by 5,556

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

Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.

Open access
Cleveland, D W, Fischer, S G, Kirschner, M W, Laemmli, U K·1977·Journal of Biological Chemistry

Abstract

A rapid and convenient method for peptide mapping of proteins has been developed. The technique, which is especially suitable for analysis of proteins that have been isolated from gels containg sodium dodecyl sulfate, involves partial enzymatic proteolysis in the presence of sodium dodecyl sulfate and analysis of the cleavage products by polyacrylamide gel electrophoresis. The pattern of peptide fragments produced is characteristic of the protein substrate and the proteolytic enzyme and is highly reproducible. Several common proteases have been used including chymotrypsin, Staphylococcus aureus protease, and papain.

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Crossref · 10.1016/s0021-9258(19)75212-0

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Metadata

Authors
Cleveland, D. W., Fischer, S. G., Kirschner, M. W., & Laemmli, U. K.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1977-02
Volume
252
Issue
3
Pages
1102-1106
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2164358316
Cited by
5,556
References
1
FWCI
155.02
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. https://app.cochat.ai/papers/10.1016/s0021-9258(19)75212-0
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Cleveland, D. W., Fischer, S. G., Kirschner, M. W., & Laemmli, U. K. (1977). Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)75212-0

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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.