Abstract
A CONVENIENT method for following the binding of a colourless competitive inhibitor I1 to an enzyme is to use a second, coloured, inhibitor I2 which is known to bind at the active site. If a spectral change is associated with the interaction between I2 and the enzyme, the gradual replacement of I2 as successive amounts of I1 are added to a mixture of it and the enzyme can be demonstrated. The acridine dye, proflavin, has been used in this way1 with α-chymotrypsin, and it has been suggested that the spectral change can be used to follow conformational changes at the enzyme site during the catalytic process. The azo-dye Biebrich scarlet (I) 
can be used similarly with, for example, α-chymotrypsin2 and lysozyme3.
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HAGUE, D., HENSHAW, J., JOHN, V. et al. Dimerization of Biebrich Scarlet and the Monomer–α-Chymotrypsin Interaction. Nature 229, 190–191 (1971). https://doi.org/10.1038/229190a0
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DOI: https://doi.org/10.1038/229190a0
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