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Differences in protein staining by Coomassie Brilliant Blue and neutron activated Coomassie Brilliant Blue dyes
Author(s) -
Gersten Douglas M.,
Wolf Pamela H.,
Zapolski Edward J.
Publication year - 1987
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.1150081202
Subject(s) - coomassie brilliant blue , staining , chemistry , amino acid , chromatography , electrophoresis , biochemistry , biology , genetics
The degree of interaction between protein and stains depends in large part upon the protein's content of basic amino acids. We have compared “staining” characteristics of Coomassie Brilliant Blue R‐250 with a dye that was rendered radioactive by neutron bombardment. The protein‐dye intensities were compared to amino acid composition as in our previous study ( Electrophoresis 1986, 7 , 327–332). While the data for “colored” dye reflected involvement of basic amino acid residues, quite unexpectedly, the radioactive dye appeared to act in part with the acidic amino acids. This may be due to enhanced binding of dye impurities or radiolysis products.