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Interference of the carbohydrate moiety in Coomassie Brilliant Blue R‐250 protein staining
Author(s) -
Osset Miquel,
Piñol Montserrat,
Fallon Martin J. M.,
De Llorens Rafael,
Cuchillo Claudi M.
Publication year - 1989
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.1150100412
Subject(s) - coomassie brilliant blue , bovine pancreatic ribonuclease , ribonuclease , glycoprotein , chemistry , staining , glycosylation , ovalbumin , biochemistry , chromatography , carbohydrate , moiety , pancreatic ribonuclease , biology , organic chemistry , antigen , rna , genetics , gene
The binding of Coomassie Brilliant Blue R‐250 to several species of bovine pancreatic ribonuclease is affected by the presence of a carbohydrate moiety in the enzyme molecule. Enzymic deglycosylation of several chromatographic fractions of ribonuclease, which have different degrees of glycosylation, results in increased staining by Coomassie Brilliant Blue R‐250. Ovalbumin and other glycoproteins tested show similar behavior. The results indicate that carbohydrate moieties may represent a common hindrance to the binding of Coomassie Brilliant Blue dyes to glycoproteins.