当总底物浓度和游离底物浓度不近似相等时结合参数的测定。
The determination of binding parameters when the total and free substrate concentrations are not approximately equal.
作者信息
Gains N
出版信息
Biochem J. 1979 Jun 1;179(3):697-700. doi: 10.1042/bj1790697.
Abstract
By using a standard graphical method values of Km and V may be found that are independent of the conditions and assumptions that the total substrate concentration approximates to its free concentration and that Km is much larger than the enzyme concentration. The procedure is also applicable to the determination of equilibrium binding parameters of a ligand to a macromolecule.
摘要
通过使用一种标准的图解法，可以得到与总底物浓度近似于其游离浓度以及Km远大于酶浓度这些条件和假设无关的Km和V值。该方法也适用于测定配体与大分子的平衡结合参数。
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引用本文的文献
1
A method for determining kinetic parameters at high enzyme concentrations.一种在高酶浓度下测定动力学参数的方法。
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2
The error in the Michaelis-Menten equation when substrate depletion by binding to the enzyme is not taken into account.米氏方程中未考虑底物因与酶结合而消耗时的误差。
Biochem J. 1992 Apr 15;283 ( Pt 2)(Pt 2):623-4. doi: 10.1042/bj2830623.
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The partial purification and properties of animal and plant hydantoinases.动植物海因酶的部分纯化及特性
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GRAPHICAL DETERMINATION OF EQUILIBRIUM CONSTANTS.平衡常数的图形测定
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The graphical determination of K m and K i .米氏常数（Km）和抑制常数（Ki）的图形测定
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Determination of dissociation and Michaelis constants at near-equal enzyme-substrate concentrations.在酶与底物浓度近似相等时解离常数和米氏常数的测定
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A more general definition of Km [proceedings].Km的更通用定义[会议记录]
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