THE RELATIONSHIP BETWEEN MICHAELIS CONSTANTS, MAXIMUM VELOCITIES AND THE EQUILIBRIUM CONSTANT FOR AN ENZYME-CATALYZED REACTION
THE RELATIONSHIP BETWEEN MICHAELIS CONSTANTS, MAXIMUM VELOCITIES AND THE EQUILIBRIUM CONSTANT FOR AN ENZYME-CATALYZED REACTION
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DOI：
10.1021/ja01104a045
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发表时间：
1953-01-01
影响因子：
15
通讯作者：
ALBERTY, RA
中科院分区：
文献类型：
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作者：
ALBERTY, RA
KiK3= A2A,(l) ß 3~ A7A9 该机制的稳态处理不会产生初始速度倒数和底物初始浓度倒数之间的线性关系。这一结论与 Segal、Kachmar 和 Boyer8 的结论一致，他们对涉及辅酶或激活剂的许多机制进行了稳态处理。
KiK3= A2A,(l) ß 3~ A7A9 The steady state treatment of this mechanism does not yield a linear relationship between the reciprocal initial velocity and the reciprocal initial concentrations of substrates. This conclusion is in agreement with that of Segal, Kachmar and Boyer8 who have giventhe steady state treatments for a number of mechanisms involving coenzymes or activators.