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Dynamics of Lysozyme-Saccharide Interactions

From the ¹ From the Department of Chemistry and Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

The interaction of lysozyme with di- and with tri-N-acetylglucosamine has been studied by the temperature jump relaxation method at pH 6.0, approximately 28.7°, ionic strength = 0.1 m. A single relaxation process is observed in the time range of 10 µsec to 100 msec, in both di- and trisaccharide-lysozyme solutions. No relaxation process is observed in the same time range in lysozyme solutions not containing saccharides. The bimolecular rate constants (k₁) and dissociation rate constants (k_-1) have been obtained for the lysozyme-saccharide interactions from the concentration dependence of the relaxation times. The rate constants (k₁) are virtually identical (4.5 x 10⁶ m^-1 sec^-1) for both the di- and the trisaccharide-lysozyme interaction, but the dissociation rate constant (k_-1) for the disaccharide is over 30 times larger than that for the trisaccharide. The ratio of rate constants k₁/k_-1 is in good agreement with apparent binding constants obtained independently by other methods. A molecular explanation of these results is given in terms of the recent crystallographic data on lysozyme-saccharide complexes.

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				D. M. Chipman and N. Sharon Mechanism of Lysozyme Action Science, August 1, 1969; 165(3892): 454 - 465. [PDF]