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ITC data fitted using a two sets of sites binding model presented a similar picture. The intrinsic fluorescence quenching data indicate that DLL-II exhibits weak binding to Gal in the presence of (NHâ‚„)â‚‚SOâ‚„ with a stoichiometry of one bound ligand per dimer. Comparison of the near-UV CD spectra with and without bound sugar revealed ligand induced conformational changes. Circular dichroism, isothermal titration calorimetry and fluorescence quenching were used to assess the sugar binding in the presence of (NHâ‚„)â‚‚Oâ‚„. The lectin is unusual in that it binds galactose (Gal), lactose (Lac) and N-acetylgalactosamine (GalNAc) only in the presence of (NHâ‚„)â‚‚SOâ‚„ and exhibits negative cooperativity and half-of-the-sites binding. The field bean (Dolichos lablab) lectin designated as PPO-haemagglutinin ( DLL-II) is bifunctional, exhibiting both polyphenol oxidase and haemagglutinating activity. The D-galactose specific lectin of field bean (Dolichos lablab) seed binds sugars with extreme negative cooperativity and half-of-the-sites binding.