首页> 外文期刊>Journal of enzyme inhibition and medicinal chemistry. >A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K-2[B3O3F4OH]
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A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K-2[B3O3F4OH]

机译:二氧化钾三元羟基氢氟丙酸K-2 [B3O3F4OH]过氧化氢酶抑制的研究

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In the development of boronic acid-based enzyme inhibitors as potential pharmaceutical drugs, dipotassium trioxohydroxytetrafluorotriborate K-2[B3O3F4OH] was listed as a promising new therapeutic for treatment of these diseases. The catalase-mediated conversion of hydrogen peroxide, in the presence and absence of K-2[B3O3F4OH] was studied. The kinetics conformed to the Michaelis-Menten model. Lineweaver-Burk plots were linear and plotted the family of straight lines intersected on the abscissa indicating non-competitive inhibition of the catalase. It appears that in the absence of inhibitor, catalase operates the best at conditions around pH 7.1 and in the presence of K-2[B3O3F4OH] the optimum is around pH 6.2. The uncatalyzed reaction of hydrogen peroxide decomposition generally has a value of activation energy of 75 kJ mole(-1), whereas catalase, in the absence of inhibitor, lowers the value to 11.2 kJ mole(-1), while in the presence 69 mmoles L-1 of K-2[B3O3F4OH] it was 37.8 kJ mole(-1)
机译:在硼酸基酶抑制剂的发展中作为潜在的药物药物,将二元羟基羟基四氟丙二醇丙酸酯K-2 [B3O3F4OH]列为治疗这些疾病的有希望的新治疗方法。研究了过氧化氢酶介导的过氧化氢转化,在k-2 [B3O3F4OH]的存在和不存在中。动力学符合Michaelis-Menten模型。 LineWeaver-Burk图是线性的,并绘制在横坐标上相交的直线系列,所述横坐标表明所述过氧化度酶的非竞争性抑制。看似在没有抑制剂的情况下,过氧氢酶在pH 7.1周围的条件下保持最佳,并且在K-2 [B3O3F4OH]存在下,最佳是在pH6.2周围。过氧化氢分解的未含析反应通常具有75kJ摩尔(-1)的活化能的值,而在没有抑制剂的情况下,过氧化氢酶降低到11.2 kJ摩尔(-1)的值,而在存在69毫摩尔K-2 [B3O3F4OH]的L-1是37.8 kJ摩尔(-1)

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