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相似文献

1
Kinetics of protein modification reactions.蛋白质修饰反应的动力学
Biochem J. 1984 Jan 15;217(2):341-51. doi: 10.1042/bj2170341.
2
Quantitative considerations of the consequences of an interplay between ligand binding and reversible adsorption of a macromolecular solute.
J Theor Biol. 1982 Sep 21;98(2):171-87. doi: 10.1016/0022-5193(82)90257-0.
3
Individual breathing reactions measured by functional labeling and hydrogen exchange methods.通过功能标记和氢交换方法测量的个体呼吸反应。
Methods Enzymol. 1986;131:508-17. doi: 10.1016/0076-6879(86)31053-x.
4
Molecular and biological constraints on ligand-binding affinity and specificity.配体结合亲和力和特异性的分子与生物学限制因素。
Biopolymers. 1997;44(2):181-98. doi: 10.1002/(SICI)1097-0282(1997)44:2<181::AID-BIP5>3.0.CO;2-R.
5
Hydrogen-exchange strategies applied to energetics of intermediate processes in protein folding.
Methods Enzymol. 2004;380:328-49. doi: 10.1016/S0076-6879(04)80015-6.
6
Thermodynamics of Bioreactions.生物反应的热力学
Annu Rev Chem Biomol Eng. 2016 Jun 7;7:395-414. doi: 10.1146/annurev-chembioeng-080615-034704.
7
Slow transitions and hysteretic behavior in enzymes.酶中的缓慢转变和滞后行为。
Annu Rev Biochem. 1979;48:471-89. doi: 10.1146/annurev.bi.48.070179.002351.
8
[Theory of multiple equilibria for polymers].[聚合物的多重平衡理论]
Biochimie. 1973;55(9):1159-62. doi: 10.1016/s0300-9084(73)80455-9.
9
Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions.热容变化能准确预测酶催化反应中的振动耦合。
FEBS Lett. 2015 Aug 4;589(17):2200-6. doi: 10.1016/j.febslet.2015.06.042. Epub 2015 Jul 11.
10
[Derivation of rate equations for the reactions catalysed by oligomeric enzymes].
Mol Biol (Mosk). 1982 Nov-Dec;16(6):1271-8.

引用本文的文献

1
Downregulation of miR-223 promotes HMGB2 expression and induces oxidative stress to activate JNK and promote autophagy in an in vitro model of acute lung injury.在急性肺损伤体外模型中，miR-223的下调促进HMGB2表达并诱导氧化应激以激活JNK并促进自噬。
J Inflamm (Lond). 2021 Nov 3;18(1):29. doi: 10.1186/s12950-021-00295-3.
2
Diethylpyrocarbonate inhibition of vacuolar H+-pyrophosphatase possibly involves a histidine residue.焦碳酸二乙酯对液泡H⁺-焦磷酸酶的抑制作用可能涉及一个组氨酸残基。
J Protein Chem. 2002 Jan;21(1):51-8. doi: 10.1023/a:1014183100021.
3
The kinetics of non-stoichiometric bursts of beta-lactam hydrolysis catalysed by class C beta-lactamases.C类β-内酰胺酶催化的β-内酰胺水解非化学计量爆发动力学。
Biochem J. 1993 Oct 1;295 ( Pt 1)(Pt 1):295-304. doi: 10.1042/bj2950295.
4
Characterization of the type I dehydroquinase from Salmonella typhi.伤寒沙门氏菌I型脱氢奎尼酸酶的特性分析。
Biochem J. 1993 Oct 1;295 ( Pt 1)(Pt 1):277-85. doi: 10.1042/bj2950277.
5
Kinetic study of an enzyme-catalysed reaction in the presence of novel irreversible-type inhibitors that react with the product of enzymatic catalysis.在存在与酶催化产物发生反应的新型不可逆型抑制剂的情况下，对酶催化反应进行动力学研究。
Bull Math Biol. 1995 Jan;57(1):157-68. doi: 10.1007/BF02458321.
6
Effect of ligands on chemical modification of proteins.配体对蛋白质化学修饰的影响。
Biochem J. 1984 Nov 1;223(3):933-4. doi: 10.1042/bj2230933.
7
Kinetics of protein modification reactions. Plot of fractional enzyme activity versus extent of protein modification in cases where all modifiable groups are essential for enzyme activity.蛋白质修饰反应动力学。在所有可修饰基团对酶活性均至关重要的情况下，酶活性分数与蛋白质修饰程度的关系图。
Biochem J. 1984 Oct 1;223(1):259-62. doi: 10.1042/bj2230259.
8
Kinetics of protein modification and enzyme inactivation reactions: interpretation of reaction order.蛋白质修饰和酶失活反应的动力学：反应级数的解释
Biochem J. 1985 Oct 15;231(2):493-4. doi: 10.1042/bj2310493.
9
Kinetics of protein-modification reactions. Stoichiometry of modification-produced enzyme inactivation: modification of rhodanese by 2,4,6-trinitrobenzenesulphonic acid.蛋白质修饰反应的动力学。修饰导致酶失活的化学计量：2,4,6-三硝基苯磺酸对硫氰酸酶的修饰
Biochem J. 1985 Aug 15;230(1):89-93. doi: 10.1042/bj2300089.
10
Chemical modification of enzymes: reaction with an unstable inhibitor.酶的化学修饰：与不稳定抑制剂的反应
Biochem J. 1985 May 1;227(3):1025-7. doi: 10.1042/bj2271025.

本文引用的文献

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The Combinations of Haemoglobin with Oxygen and with Carbon Monoxide. I.血红蛋白与氧气及一氧化碳的结合。I.
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The Oxygen Equilibrium of Hemoglobin and Its Structural Interpretation.血红蛋白的氧平衡及其结构解析
Proc Natl Acad Sci U S A. 1935 Apr;21(4):186-91. doi: 10.1073/pnas.21.4.186.
3
Some properties of specific cholinesterase with particular reference to the mechanism of inhibition by diethyl p-nitrophenyl thiophosphate (E 605) and analogues.特异性胆碱酯酶的某些特性，特别涉及对硫代磷酸O,O-二乙基对硝基苯酯（E605）及其类似物的抑制机制。
Biochem J. 1950 Apr;46(4):451-60. doi: 10.1042/bj0460451.
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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.关于别构转变的本质：一个合理的模型。
J Mol Biol. 1965 May;12:88-118. doi: 10.1016/s0022-2836(65)80285-6.
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INACTIVATION OF MYOSIN BY 2,4-DINITROPHENOL AND PROTECTION BY ADENOSINE TRIPHOSPHATE AND OTHER PHOSPHATE COMPOUNDS.2,4-二硝基苯酚对肌球蛋白的失活作用以及三磷酸腺苷和其他磷酸盐化合物的保护作用
J Biol Chem. 1963 Nov;238:3654-9.
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Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase.甲磺酸酯作为乙酰胆碱酯酶的不可逆抑制剂
J Biol Chem. 1962 Oct;237:3245-9.
7
Relation between modification of functional groups of proteins and their biological activity. I.A graphical method for the determination of the number and type of essential groups.蛋白质官能团修饰与其生物活性之间的关系。I. 一种确定必需基团数量和类型的图解方法。
Sci Sin. 1962 Nov;11:1535-58.
8
A method for characterizing the type and numbers of groups involved in enzyme action.一种表征参与酶作用的基团类型和数量的方法。
J Biol Chem. 1961 Jul;236:1973-9.
9
Kinetics of irreversible enzyme inhibition: the interpretation of the fractional enzyme activity vs. extent of protein modification plot.不可逆酶抑制动力学：酶活性分数与蛋白质修饰程度关系图的解读
J Theor Biol. 1980 Aug 7;85(3):553-60. doi: 10.1016/0022-5193(80)90328-8.
10
Effect of ligand on chemical modification of proteins. Graphical determinations of dissociation constant and number of essential residues affected by ligand binding.配体对蛋白质化学修饰的影响。通过图形法测定解离常数以及受配体结合影响的必需残基数量。
J Theor Biol. 1980 Jun 21;84(4):691-708. doi: 10.1016/s0022-5193(80)80028-2.

Kinetics of protein modification reactions.

作者信息

Rakitzis E T

出版信息

Biochem J. 1984 Jan 15;217(2):341-51. doi: 10.1042/bj2170341.

DOI:10.1042/bj2170341
PMID:6365085
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1153224/
Abstract
摘要