Thompson R B, Lakowicz J R
Biochim Biophys Acta. 1984 Oct 9;790(1):87-90. doi: 10.1016/0167-4838(84)90335-2.
The equilibrium binding of 4-methylumbelliferyl alpha-D-mannopyranoside to concanavalin A was measured by changes in fluorescence quenching observed at pressures ranging from 1 to 2000 bar (1974 atmospheres). From the pressure-induced changes in the apparent Ka, we calculated volume changes for the association reaction of -2.5 and -1.7 +/- 1 ml/mol for concanavalin A in its dimeric and tetrameric forms, respectively. This carbohydrate-binding reaction is less pressure-sensitive than other protein-ligand interactions that have been studied under pressure. The volume change observed is comparable to that expected for a reaction involving hydrogen bond formation, in a non-polar environment.
通过在1至2000巴（1974个大气压）的压力范围内观察到的荧光猝灭变化，测定了4-甲基伞形酮基α-D-甘露吡喃糖苷与伴刀豆球蛋白A的平衡结合。根据压力诱导的表观解离常数（Ka）变化，我们分别计算出二聚体形式和四聚体形式的伴刀豆球蛋白A缔合反应的体积变化为-2.5和-1.7±1毫升/摩尔。这种碳水化合物结合反应比在压力下研究的其他蛋白质-配体相互作用对压力的敏感性更低。观察到的体积变化与在非极性环境中涉及氢键形成的反应预期的体积变化相当。
