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On the relationship of amino acid composition to silver staining of proteins in electrophoresis gels: II. Peptide sequence analysis
Author(s) -
Gersten Douglas M.,
Rodriguez Lewis V.,
George David G.,
Johnston Dennis A.,
Zapolski Edward J.
Publication year - 1991
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150120605
Subject(s) - silver stain , tripeptide , staining , peptide , electrophoresis , biochemistry , chemistry , gel electrophoresis of proteins , gel electrophoresis , polyacrylamide gel electrophoresis , amino acid , peptide sequence , sequence (biology) , chromatography , biology , microbiology and biotechnology , genetics , enzyme , gene
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 diferences in di‐ or tripeptide composition. The results indicate that some order of protein structure other than short peptides accounts for the staining differences observed.