Osset M, Piñol M, Fallon M J, de Llorens R, Cuchillo C M
Institut de Biologia Fonamental, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
Electrophoresis. 1989 Apr;10(4):271-3. doi: 10.1002/elps.1150100412.
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.
考马斯亮蓝R - 250与几种牛胰核糖核酸酶的结合受到酶分子中碳水化合物部分的影响。对核糖核酸酶不同糖基化程度的几个色谱级分进行酶促去糖基化处理后，考马斯亮蓝R - 250的染色增强。所测试的卵清蛋白和其他糖蛋白也表现出类似行为。结果表明，碳水化合物部分可能是考马斯亮蓝染料与糖蛋白结合的常见阻碍因素。
