On the relationship of amino acid composition to silver staining of proteins in electrophoresis gels: II. Peptide sequence analysis

The quantification of proteins in silver-stained electrophoresis gels has been limited by the differences in "stainability" of different proteins. Despite efforts by many researchers, the precise basis of the reaction between silver reagents and polypeptides is still unclear, and, dependin...

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Bibliographic Details
Published inElectrophoresis Vol. 12; no. 6; p. 409
Main Authors Gersten, D M, Rodriguez, L V, George, D G, Johnston, D A, Zapolski, E J
Format Journal Article
LanguageEnglish
Published Germany 1991
Subjects
Amino Acid Sequence
Amino Acids - chemistry
Electrophoresis, Polyacrylamide Gel
Peptides - chemistry
Protein Conformation
Silver
Staining and Labeling
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Summary:The quantification of proteins in silver-stained electrophoresis gels has been limited by the differences in "stainability" of different proteins. Despite efforts by many researchers, the precise basis of the reaction between silver reagents and polypeptides is still unclear, and, depending on the formulation, may even differ. We have tested the hypothesis that differences in stainability among proteins can be attributed to differences in di- or tripeptide composition. The results indicate that some order of protein structure other than short peptides accounts for the staining differences observed.
ISSN:0173-0835
DOI:10.1002/elps.1150120605