Böhme H J, Schellenberger W, Retterrath P, Hofmann E, Misselwitz R
Acta Biol Med Ger. 1975;34(9):1447-51.
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.
