title: On the relationship of amino acid composition to silver staining of proteins in electrophoresis gels: II. Peptide sequence analysis.
abstract: 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.
authors.affiliation: Department of Pathology, Georgetown University Medical Center, Washington, DC 20007.
authors.forename: D M
authors.initials: DM
authors.lastname: Gersten
authors.forename: L V
authors.initials: LV
authors.lastname: Rodriguez
authors.forename: D G
authors.initials: DG
authors.lastname: George
authors.forename: D A
authors.initials: DA
authors.lastname: Johnston
authors.forename: E J
authors.initials: EJ
authors.lastname: Zapolski
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D012834:Silver; D013194:Staining and Labeling
chemical_list: D000596:Amino Acids; D010455:Peptides; D012834:Silver