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Negatively co-operative ligand binding.负协同配体结合
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2
Curves of ligand binding. The use of hyperbolic functions for expressing titration curves.配体结合曲线。使用双曲线函数来表达滴定曲线。
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3
Minimal models of multi-site ligand-binding kinetics.多位点配体结合动力学的最小模型
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4
Analysis of ligand-binding data without knowledge of bound or free ligand molar concentration.在不知道结合或游离配体摩尔浓度的情况下分析配体结合数据。
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5
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。
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6
[Cooperation effects in binding of large ligands to DNA. II. Contact interactions between adsorbed ligands].[大配体与DNA结合中的协同效应。II. 吸附配体之间的接触相互作用]
Mol Biol (Mosk). 1984 Jul-Aug;18(4):1066-80.
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A new approach to the measurement of sigmoid curves with enzyme kinetic and ligand binding data.一种利用酶动力学和配体结合数据测量S形曲线的新方法。
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Correcting binding parameters for interacting ligand-lattice systems.修正相互作用配体晶格体系的结合参数。
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Interconversion of the ligand arrays in the CD and EF sites of oncomodulin. Influence on Ca2+-binding affinity.癌调蛋白CD和EF位点配体阵列的相互转换。对Ca2+结合亲和力的影响。
Biochemistry. 1998 Jun 23;37(25):9101-11. doi: 10.1021/bi973151w.
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Modulation of protein function by exogenous ligands in protein cavities: CO binding to a myoglobin cavity mutant containing unnatural proximal ligands.蛋白质腔中外源配体对蛋白质功能的调节:一氧化碳与含有非天然近端配体的肌红蛋白腔突变体的结合
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引用本文的文献

1
Parameter Reliability and Understanding Enzyme Function.参数可靠性与酶功能理解。
Molecules. 2022 Jan 1;27(1):263. doi: 10.3390/molecules27010263.
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Graphical determination of pK values of the active-site groups of enzymes. An analysis of the bell-shaped curves.酶活性位点基团pK值的图形测定。钟形曲线分析。
Biochem J. 1980 Mar 1;185(3):609-10. doi: 10.1042/bj1850609.
3
Iodothyronine 5'-deiodinase in rat kidney microsomes. Kinetic behavior at low substrate concentrations.大鼠肾微粒体中的碘甲状腺原氨酸5'-脱碘酶。低底物浓度下的动力学行为。
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Kinetics of the hydrolysis of N-benzoyl-L-serine methyl ester catalysed by bromelain and by papain. Analysis of modifier mechanisms by lattice nomography, computational methods of parameter evaluation for substrate-activated catalyses and consequences of postulated non-productive binding in bromelain- and papain-catalysed hydrolyses.菠萝蛋白酶和木瓜蛋白酶催化N-苯甲酰-L-丝氨酸甲酯水解的动力学。通过晶格列线图分析修饰机制、底物活化催化的参数评估计算方法以及菠萝蛋白酶和木瓜蛋白酶催化水解中假定的非生产性结合的后果。
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5
Curves of ligand binding. The use of hyperbolic functions for expressing titration curves.配体结合曲线。使用双曲线函数来表达滴定曲线。
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6
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8
The origin of multiply sigmoid curves of pH-dependence. The partitioning of groups among titration pK values.pH依赖性多重S形曲线的起源。各基团在滴定pK值间的分配。
Biochem J. 1991 Aug 15;278 ( Pt 1)(Pt 1):279-84. doi: 10.1042/bj2780279.
9
Factorization of the Michaelis functions.米氏函数的因式分解。
Biochem J. 1975 Nov;151(2):271-4. doi: 10.1042/bj1510271.
10
Sigmoid curves, non-linear double-reciprocal plots and allosterism.S形曲线、非线性双倒数图与别构效应
Biochem J. 1975 Aug;149(2):313-28. doi: 10.1042/bj1490313.

本文引用的文献

1
[SOME EVIDENCE FOR AN ALLOSTERIC EFFECT DURING TRYPTIC HYDROLYSIS OF P-TOLUENESULFONYL-L-ARGININE METHYL ESTER].[对甲苯磺酰-L-精氨酸甲酯胰蛋白酶水解过程中别构效应的一些证据]
Biochim Biophys Acta. 1964 Jul 8;89:117-26.
2
SUBSTRATE ACTIVATION OF TRYPSIN.胰蛋白酶的底物激活作用。
Biochemistry. 1963 Jul-Aug;2:843-50. doi: 10.1021/bi00904a037.
3
On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction.关于酶催化反应最大初始速度的pH变化的解释
Biochim Biophys Acta. 1954 Mar;13(3):347-53. doi: 10.1016/0006-3002(54)90340-6.
4
Shapes of curves of pH-dependence of reactions.反应pH依赖性曲线的形状。
Biochem J. 1973 Jan;131(1):149-54. doi: 10.1042/bj1310149.
5
Substrate activation of trypsin and acetyltrypsin caused by -N-benzoyl-L-arginine p-nitroanilide.对硝基苯甲酰-L-精氨酸甲酯引起的胰蛋白酶和乙酰胰蛋白酶的底物激活作用。
J Biochem. 1972 Aug;72(2):281-90. doi: 10.1093/oxfordjournals.jbchem.a129907.
6
Anomalous kinetics observed in the catalysis of a peptide substrate with collagenase.在用胶原酶催化肽底物时观察到异常动力学。
Biochim Biophys Acta. 1972 Dec 7;289(2):401-4. doi: 10.1016/0005-2744(72)90092-7.
7
Models for cooperative effects in proteins containing subunits. Effects of two interacting ligands.含亚基蛋白质中协同效应的模型。两个相互作用配体的效应。
J Biol Chem. 1967 Sep 25;242(18):4192-205.

负协同配体结合

Negatively co-operative ligand binding.

作者信息

Dixon H B, Tipton K F

出版信息

Biochem J. 1973 Aug;133(4):837-42. doi: 10.1042/bj1330837.

DOI:10.1042/bj1330837
PMID:4748836
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1177774/
Abstract

Simple systems are considered in which the binding of a ligand at a single site exhibits a doubly sigmoid curve when saturation is plotted against the logarithm of ligand concentration, i.e. where a fraction of the site exhibits one dissociation constant and the rest exhibits another. The condition for this to occur is that the ligand should also combine at another site on the binding molecule with comparable affinity and that the binding at one site should markedly lower affinity at the other. The protonation of simple compounds such as cysteine and 3-hydroxypyridine is taken as an example of this process and the equations derived are also applied to the binding of substrates to enzymes.

摘要

我们考虑这样一些简单系统,其中当以配体浓度的对数为横坐标绘制饱和度曲线时,单个位点上配体的结合呈现出双S形曲线,也就是说,一部分位点表现出一个解离常数,其余位点表现出另一个解离常数。发生这种情况的条件是,配体还应以相当的亲和力结合在结合分子的另一个位点上,并且一个位点上的结合应显著降低另一个位点的亲和力。以半胱氨酸和3-羟基吡啶等简单化合物的质子化作为该过程的一个例子,推导得到的方程也适用于底物与酶的结合。