Effect of phosphate concentration on the kinetics of bovine liver glutamate dehydrogenase self-association

Ryoichi Tashiro, Akie Nishimura, Tohru Inoue, Ryosuke Shimozawa
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引用次数: 5

Abstract

The kinetics of the self-association of bovine liver glutamate dehydrogenase was studied at various phosphate buffer concentrations (pH 7.3) at 11.5°C by means of the temperature-jump technique with scattered light detection. The observed relaxation times were well explained by the random association model of Thusius et al. With increasing phosphate concentration, the association rate constant derived from the model decreased, while the dissociation rate constant was left almost constant. Relaxation amplitude was also dependent on the phosphate concentration. The changes in the rate constant and relaxation amplitude with phosphate concentration are well elucidated by assuming that glutamate dehydrogenase is protected from association by specific masking of the association site by phosphate ions.

磷酸盐浓度对牛肝谷氨酸脱氢酶自结合动力学的影响
采用跳温散射光检测技术,在11.5℃条件下,研究了不同磷酸盐缓冲液浓度(pH 7.3)下牛肝谷氨酸脱氢酶的自结合动力学。观察到的松弛时间可以用Thusius等人的随机关联模型很好地解释。随着磷酸盐浓度的增加,模型得到的缔合速率常数减小,而解离速率常数基本保持不变。松弛幅度也依赖于磷酸盐浓度。速率常数和弛豫振幅随磷酸盐浓度的变化可以很好地解释,假设谷氨酸脱氢酶通过磷酸盐离子特异性掩蔽结合位点来保护其不发生结合。
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