Interference of the carbohydrate moiety in Coomassie Brilliant Blue R‐250 protein staining

Miquel Osset; Montserrat Piñol; Martin J.M. Fallon; Rafael De Llorens; Claudi M. Cuchillo

doi:10.1002/elps.1150100412

Interference of the carbohydrate moiety in Coomassie Brilliant Blue R‐250 protein staining

Miquel Osset, Montserrat Piñol, Martin J.M. Fallon, Rafael De Llorens, Claudi M. Cuchillo

Department of Biochemistry and Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

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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
Pages (from-to)	271-273
Journal	ELECTROPHORESIS
Volume	10
Issue number	4
DOIs	https://doi.org/10.1002/elps.1150100412
Publication status	Published - 1 Jan 1989

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@article{c069f258de944d5f961d08fab17a28a7,

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. Copyright {\textcopyright} 1989 VCH Verlagsgesellschaft mbH",

author = "Miquel Osset and Montserrat Pi{\~n}ol and Fallon, {Martin J.M.} and {De Llorens}, Rafael and Cuchillo, {Claudi M.}",

year = "1989",

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doi = "10.1002/elps.1150100412",

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TY - JOUR

T1 - Interference of the carbohydrate moiety in Coomassie Brilliant Blue R‐250 protein staining

AU - Osset, Miquel

AU - Piñol, Montserrat

AU - Fallon, Martin J.M.

AU - De Llorens, Rafael

AU - Cuchillo, Claudi M.

PY - 1989/1/1

Y1 - 1989/1/1

N2 - 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

AB - 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

U2 - 10.1002/elps.1150100412

DO - 10.1002/elps.1150100412

M3 - Article

VL - 10

SP - 271

EP - 273

JO - Electrophoresis

JF - Electrophoresis

SN - 0173-0835

IS - 4

ER -

Interference of the carbohydrate moiety in Coomassie Brilliant Blue R‐250 protein staining

Abstract

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