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

The Journal of biological chemistry (1977-02-10)
D W Cleveland, S G Fischer, M W Kirschner, U K Laemmli
PMID320200
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.

MATERIALS
Product Number
Brand
Product Description

Supelco
Sodium dodecyl sulfate, suitable for ion pair chromatography, LiChropur, ≥99.0%
Sigma-Aldrich
Endoproteinase Glu-C from Staphylococcus aureus V8, Type XVII-B, lyophilized powder, 500-1,000 units/mg solid