Datta G, Naik S S, Gurnani S
Int J Lepr Other Mycobact Dis. 1985 Sep;53(3):428-32.
The binding of dapsone to hen egg white lysozyme has been studied using fluorescence spectroscopy. At low concentrations the drug binds lysozyme with a Ka = 3.3 X 10(4) M-1 forming a 1:1 complex. At high concentrations the protein was found to bind the drug in a cooperative manner at two sites with an average association constant of 6.3 X 10(4) M-1. Both Trp-108 and Trp-62 of lysozyme are involved in the association process. Acetylation of the lysine residues increased the affinity of the drug to the protein. However, drug association showed no effect on the enzymatic activity of the protein.
已使用荧光光谱法研究了氨苯砜与鸡蛋清溶菌酶的结合情况。在低浓度下，该药物以Ka = 3.3×10⁴ M⁻¹与溶菌酶结合，形成1:1复合物。在高浓度下，发现蛋白质以协同方式在两个位点结合该药物，平均缔合常数为6.3×10⁴ M⁻¹。溶菌酶的Trp-108和Trp-62均参与缔合过程。赖氨酸残基的乙酰化增加了药物与蛋白质的亲和力。然而，药物缔合对蛋白质的酶活性没有影响。
