Halvorson H R
Biochemistry. 1979 Jun 12;18(12):2480-7. doi: 10.1021/bi00579a007.
The kinetics of self-association for beef liver glutamate dehydrogenase (EC 1.4.1.3) have been measured by using pressure perturbation in both the time domain and the frequency domain by monitoring scattered light intensity. The kinetic behavior is entirely consistent with the random self-association model proposed by Thusius et al. [Thusius, D., Dessen, P., & Jallon, J. M. (1975) J. Mol. Biol. 92, 413--432]. The activation volume deltaV for association is estimated to be positive, and it is shown that this provides further corroboration of the molecular mechanism advanced by these same authors. A rapid shift in scattered light intensity is attributed to preferential interaction between the phosphate anion and the protein, proceeding with a positive volume change (2--5 mL/mol of phosphate). A description of the instrument developed for this study is also included.
通过在时域和频域中利用压力扰动监测散射光强度，测定了牛肝谷氨酸脱氢酶（EC 1.4.1.3）的自缔合动力学。动力学行为与Thusius等人提出的随机自缔合模型[Thusius, D., Dessen, P., & Jallon, J. M. (1975) J. Mol. Biol. 92, 413--432]完全一致。缔合的活化体积ΔV估计为正值，并且表明这进一步证实了这些作者提出的分子机制。散射光强度的快速变化归因于磷酸根阴离子与蛋白质之间的优先相互作用，其伴随正的体积变化（每摩尔磷酸2 - 5 mL）。还包括了为本研究开发的仪器的描述。
