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1
The determination of binding parameters when the total and free substrate concentrations are not approximately equal.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。
Biochem J. 1979 Jun 1;179(3):697-700. doi: 10.1042/bj1790697.
2
[Specific ligand induced dimerization of allosteric enzymes].[特定配体诱导变构酶的二聚化]
Mol Biol (Mosk). 1982 Mar-Apr;16(2):424-33.
3
The determination of thermodynamic allosteric parameters of an enzyme undergoing steady-state turnover.处于稳态周转的酶的热力学别构参数的测定。
Arch Biochem Biophys. 1983 Jul 1;224(1):389-401. doi: 10.1016/0003-9861(83)90225-4.
4
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。
Biochem J. 1982 Apr 1;203(1):339-42. doi: 10.1042/bj2030339.
5
Equations for progress curves of some kinetic models of enzyme-single substrate-single slow binding modifier system.酶-单底物-单慢结合调节剂系统某些动力学模型的进展曲线方程。
J Enzyme Inhib. 1998 Jun;13(3):161-76. doi: 10.3109/14756369809028338.
6
Interpreting enzyme and receptor kinetics: keeping it simple, but not too simple.解读酶与受体动力学：力求简洁，但不过于简单。
Nucl Med Biol. 2003 Nov;30(8):819-26. doi: 10.1016/s0969-8051(03)00132-x.
7
Testing and characterizing enzymes and membrane-bound carrier proteins acting on amphipathic ligands in the presence of bilayer membrane material and soluble binding protein. Application to the uptake of oleate into isolated cells.在存在双层膜材料和可溶性结合蛋白的情况下，对作用于两亲性配体的酶和膜结合载体蛋白进行检测和表征。应用于油酸进入分离细胞的摄取过程。
Biochem J. 1992 Jun 1;284 ( Pt 2)(Pt 2):353-61. doi: 10.1042/bj2840353.
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A graphical method for determining the number of essential sites in enzymes with multiple binding sites for a ligand.一种用于确定对配体具有多个结合位点的酶中必需位点数量的图解方法。
Anal Biochem. 1994 Jan;216(1):15-26. doi: 10.1006/abio.1994.1002.
9
Analysis of macromolecule--ligand binding by determination of stepwise equilibrium constants.通过测定逐步平衡常数分析大分子-配体结合
Biochemistry. 1970 Nov 10;9(23):4580-7. doi: 10.1021/bi00825a018.
10
Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: analysis of stopped-flow kinetic experiments.配体结合前大分子变构构象转变的动力学：停流动力学实验分析
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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。
Biochem J. 1982 Apr 1;203(1):339-42. doi: 10.1042/bj2030339.
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.

本文引用的文献

1
The partial purification and properties of animal and plant hydantoinases.动植物海因酶的部分纯化及特性
J Biol Chem. 1949 Dec;181(2):449-58.
2
Non-inverted versus inverted plots in enzyme kinetics.酶动力学中的非反转图与反转图
Nature. 1959 Oct 24;184:1296-8. doi: 10.1038/1841296b0.
3
GRAPHICAL DETERMINATION OF EQUILIBRIUM CONSTANTS.平衡常数的图形测定
Biochem J. 1965 Mar;94(3):760-2. doi: 10.1042/bj0940760.
4
A modified graphical method for determination of equilibrium constants.一种用于测定平衡常数的改进图形法。
Biochem J. 1966 Aug;100(2):334-5. doi: 10.1042/bj1000334.
5
The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters.直接线性作图法。一种用于估算酶动力学参数的新的图形方法。
Biochem J. 1974 Jun;139(3):715-20. doi: 10.1042/bj1390715.
6
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
Biochem J. 1972 Aug;129(1):197-202. doi: 10.1042/bj1290197.
7
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
Anal Biochem. 1977 May 1;79(1-2):643-7. doi: 10.1016/0003-2697(77)90451-1.
8
A more general definition of Km [proceedings].Km的更通用定义[会议记录]
Biochem Soc Trans. 1978;6(1):258-60. doi: 10.1042/bst0060258.
9
Steady-state enzyme kinetics in mutual depletion systems.
Biochem Soc Trans. 1979 Apr;7(2):429-39. doi: 10.1042/bst0070429.

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.

DOI:10.1042/bj1790697
PMID:475775
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1186679/
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。