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Peptide mapping of basic proteins by proteolysis in acetic acid/urea-minislab polyacrylamide gels.

作者信息

Davie J R

出版信息

Anal Biochem. 1985 Feb 1;144(2):522-6. doi: 10.1016/0003-2697(85)90149-6.

DOI:10.1016/0003-2697(85)90149-6
PMID:3887981
Abstract

A method to obtain peptide maps of basic proteins on acetic acid/urea (AU) -polyacrylamide minislab gels is presented. Basic proteins such as the histones are digested with Staphylococcus aureus V8 protease in the stacking gel (pH 4) of an AU-polyacrylamide minislab gel. As the peptides are resolved in the AU minislab gel on the basis of charge and size, it is possible to separate peptides containing modified amino acids from the unmodified, parent peptide. The peptide(s) containing the modified residue may be identified following electrophoresis on a second-dimension sodium dodecyl sulfate-polyacrylamide minislab gel. This procedure will be useful for comparing histone variants and for the study of histone modifications.

摘要

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