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Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis.
Journal of Biological Chemistry · 1977 · Vol. 252(3) · pp. 1102–1106
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.
Advanced Proteomics Techniques and ApplicationsProtein purification and stabilityRNA and protein synthesis mechanismsProteolysisSodium dodecyl sulfatePapainChemistryGel electrophoresisProteasesProteasePeptideBiochemistryChymotrypsin
MeSH terms
Alkaline PhosphataseElectrophoresis, Polyacrylamide GelEscherichia coliPeptide FragmentsPeptide HydrolasesProteinsSodium Dodecyl SulfateStaphylococcus aureusTubulin
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References
The Reliability of Molecular Weight Determinations by Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis
Journal of Biological Chemistry · 1969 · 20,334 citations
Analysis of bacteriophage T7 early RNAs and proteins on slab gels
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