抄録
The binding of N-acetyl-D-glucosamine to lysozyme [EC 3. 2. 1. 17] was studied by the circular dichroism (CD) technique. The increase in the CD band of lysozyme at 294 mμ resulting from binding of the inhibitor was utilized to study the interaction. It was found that the association was optimal at pH's 3.5 to 5.5 due to ionization of two groups with apparent pK's of about 2.5 and 6.5. The binding site of N-acetyl-glucosamine was discussed in relation to X-ray crystallographic data on lysozyme. The pH dependence of the CD spectrum in the absence of the inhibitor was also described.
