Villanueva G B, Perret V
Thromb Res. 1983 Mar 1;29(5):489-98. doi: 10.1016/0049-3848(83)90344-4.
Chemical modification studies have demonstrated that the ultra-violet difference spectrum of alpha-thrombin produced in the presence of sodium is due primarily to changes in the environment of tyrosine residues. This is based on the observation that the spectrum could be abolished by treatment of alpha-thrombin with tetranitromethane but not with dimethyl-(2-hydroxy-5-nitrobenzyl) sulfonium bromide. Although lithium produces similar (UV) difference spectrum, circular dichroism studies indicate that sodium and lithium induce different conformational transitions. alpha-Thrombin tends to assume a more ordered structure in the presence of sodium whereas lithium has the reverse effect. This inverse behavior is consistent with the effects of these cations on the autolysis rate and thermal stability of the activities of alpha-thrombin.
化学修饰研究表明,在有钠存在的情况下产生的α-凝血酶的紫外差光谱主要是由于酪氨酸残基环境的变化。这是基于以下观察结果:用四硝基甲烷处理α-凝血酶可消除该光谱,但用二甲基-(2-羟基-5-硝基苄基)溴化锍处理则不能。尽管锂产生类似的(紫外)差光谱,但圆二色性研究表明,钠和锂诱导不同的构象转变。在有钠存在的情况下,α-凝血酶倾向于呈现更有序的结构,而锂则有相反的效果。这种相反的行为与这些阳离子对α-凝血酶活性的自溶速率和热稳定性的影响是一致的。