title: Interference of the carbohydrate moiety in coomassie brilliant blue R-250 protein staining.
abstract: 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.
authors: Institut de Biologia Fonamental, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
authors: M
authors: M
authors: Osset
authors: M
authors: M
authors: Piñol
authors: M J
authors: MJ
authors: Fallon
authors: R
authors: R
authors: de Llorens
authors: C M
authors: CM
authors: Cuchillo
mesh_terms: D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins; D006031:Glycosylation; D010047:Ovalbumin; D012259:Ribonuclease, Pancreatic; D012394:Rosaniline Dyes; D012967:Sodium Dodecyl Sulfate; D013194:Staining and Labeling
chemical_list: D006023:Glycoproteins; D012394:Rosaniline Dyes; D012967:Sodium Dodecyl Sulfate; C024757:Coomassie brilliant blue R; D010047:Ovalbumin; D012259:Ribonuclease, Pancreatic