Specific binding of Cibacron blue F3G-A to yeast phosphofructokinase.
The complex formation between the ATP-analogous reactive dye Cibacron blue F3G-A and yeast phosphofructokinase is accompanied by a red shift of the visible absorption spectrum. From the position of lambdamax of the dye-phosphofructokinase complex in the polarity scales obtained from model solvents it may be concluded that the chromophoric system is evidently located in a highly apolaric range of the enzyme protein. The spectrophotometric titration of yeast phosphofructokinase with Cibacron blue F3G-A yielded a sigmoidal binding curve, which can be described by the MONOD-WYMAN-CHANGEUX model.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D002021:Buffers; D007202:Indicators and Reagents; D010732:Phosphofructokinase-1 / Q000378:metabolism*; D015003:Yeasts / Q000201:enzymology*
D002021:Buffers; D007202:Indicators and Reagents; D000255:Adenosine Triphosphate; D010732:Phosphofructokinase-1