Calcofluor White - carbohydrate residues interaction

In these three different studies, we are monitoring the same type of interaction calcofluor white - carbohydrate residues. 

The interaction between Calcofluor White and carbohydrate residues of a -acid glycoprotein depends on the secondary structure of the carbohydrate residues, with the fluorescence parameters of Calcofluor being sensitive to this spatial secondary structure. 

Albani, J.R., Sillen, A., Plancke, Y.D., Coddeville, B. and Engelborghs, Y. (2000) Interaction between carbohydrate residues of ai-acid glycoprotein (orosomucoid) and saturating concentrations of Calcofluor White. A fluorescence study. Carbohydrate Research 327, 333-340. 

The values of of a cliromophore can change whether it is free in solution or bound to a protein. This change can be important or non-significant. For example we determined the value of of calcofluor white free in solution and bound to ai-acid glycoprotein which contains 40% carbohydrate by weight. Calcofluor White binds specifically to the hydrophilic carbohydrate residues (Albani and Plancke, 1998 1999), although interaction with hydrophobic pockets of some proteins such as serum albumin occurs also (Albani and Plancke, 1998 1999). 

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