Haldane-Radić 酶动力学对传统和逻辑斯谛 Michaelis-Menten 模型的可约性。
On the reducible character of Haldane-Radić enzyme kinetics to conventional and logistic Michaelis-Menten models.
机构信息
Laboratory of Computational and Structural Physical Chemistry, Chemistry Department, West University of Timişoara, Pestalozzi Street No.16, Timisoara, RO-300115, Romania.
出版信息
Molecules. 2011 Apr 13;16(4):3128-45. doi: 10.3390/molecules16043128.
The conceptual and practical issues regarding the reduction of the Haldane-Radić enzymic mechanism, specific for cholinesterase kinetics, to the consecrated or logistically modified Michaelis-Menten kinetics, specific for some mutant enzymes, are here clarified as due to the limited initial substrate concentration, through detailed initial rate and progress curve analysis, even when other classical conditions for such equivalence are not entirely fulfilled.
有关将特定于胆碱酯酶动力学的 Haldane-Radić 酶促机制简化为特定于某些突变酶的传统或逻辑修改的 Michaelis-Menten 动力学的概念和实际问题，通过详细的初始速率和进展曲线分析，即使其他经典等效条件不完全满足，也可以阐明这些问题是由于初始底物浓度有限所致。
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