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. Copyright © 1989 VCH Verlagsgesellschaft mbH
Original language | English |
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Pages (from-to) | 271-273 |
Journal | ELECTROPHORESIS |
Volume | 10 |
Issue number | 4 |
DOIs | |
Publication status | Published - 1 Jan 1989 |