Interference of the carbohydrate moiety in coomassie brilliant blue R-250 protein staining.
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.
Osset
M
M
Institut de Biologia Fonamental, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
Piñol
M
M
Fallon
M J
MJ
de Llorens
R
R
Cuchillo
C M
CM
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
D006023:Glycoproteins; D012394:Rosaniline Dyes; D012967:Sodium Dodecyl Sulfate; C024757:Coomassie brilliant blue R; D010047:Ovalbumin; D012259:Ribonuclease, Pancreatic