• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

一种用于确定抑制常数的图形方法。

A graphical method for determining inhibition constants.

机构信息

Department of Biochemistry, Aichi Medical University School of Medicine, Nagakute, Aichi, Japan.

出版信息

J Enzyme Inhib Med Chem. 2009 Dec;24(6):1288-90. doi: 10.3109/14756360902829766.

DOI:10.3109/14756360902829766
PMID:19912063
Abstract

A new simple graphical method is described for the determination of inhibition type and inhibition constants of an enzyme reaction without any replot. The method consists of plotting experimental data as (V-v)/v versus the inhibitor concentration at two or more concentrations of substrate, where V and v represent the maximal velocity and the velocity in the absence and presence of inhibitor with given concentrations of the substrate, respectively. Competitive inhibition gives straight lines that converge on the abscissa at a point where [I] = -K(i). Uncompetitive inhibition gives parallel lines with the slope of 1/K'(i). For mixed type inhibition, the intersection in the plot is given by [I] = -K(i) and (V-v)/v = -K(i)/K'(i) in the third quadrant, and in the special case where K(i) = K'(i) (noncompetitive inhibition) the intersections occur at the point where [I] = -K(i) and (V-v)/v = -1. The present method, the "quotient velocity plot," provides a simple way of determining the inhibition constants of all types of inhibitors.

摘要

描述了一种新的简单图形方法,用于在无需任何重新绘图的情况下确定酶反应的抑制类型和抑制常数。该方法包括将实验数据绘制为(V-v)/v 与抑制剂浓度的关系,其中 V 和 v 分别表示在给定底物浓度下无抑制剂和有抑制剂时的最大速度和速度。竞争性抑制给出在 [I] = -K(i) 处收敛于横坐标的直线。非竞争性抑制给出斜率为 1/K'(i) 的平行线。对于混合抑制类型,在第三象限中,在图中的交点处 [I] = -K(i) 和 (V-v)/v = -K(i)/K'(i),在特殊情况下 K(i) = K'(i)(非竞争性抑制),交点出现在 [I] = -K(i) 和 (V-v)/v = -1 的点处。这种新的“商速度图”方法提供了一种简单的方法来确定所有类型抑制剂的抑制常数。

相似文献

1
A graphical method for determining inhibition constants.一种用于确定抑制常数的图形方法。
J Enzyme Inhib Med Chem. 2009 Dec;24(6):1288-90. doi: 10.3109/14756360902829766.
2
A new plot for multiple enzyme inhibition.一种多重酶抑制的新策略。
Biochem Int. 1983 Aug;7(2):247-53.
3
A graphical method for determining inhibition parameters for partial and complete inhibitors.一种用于确定部分抑制剂和完全抑制剂抑制参数的图解方法。
Biochem J. 1987 Dec 15;248(3):815-20. doi: 10.1042/bj2480815.
4
Rigorous determination of the Hill coefficient of non-Michaelian substrate-inhibited enzymes.非米氏底物抑制酶的希尔系数的精确测定
Biochem Int. 1988 Jul;17(1):147-54.
5
Advantages of continuous over batch reactors for the kinetic analysis of enzymes inhibited by an unknown substrate impurity.连续式反应器相较于间歇式反应器在分析受未知底物杂质抑制的酶的动力学方面的优势。
Biotechnol Bioeng. 2002 Sep 20;79(6):641-6. doi: 10.1002/bit.10326.
6
A new plot for the kinetic analysis of dead-end enzyme inhibitors.一种用于终产物酶抑制剂动力学分析的新方法。
Biochem Int. 1985 Jul;11(1):11-9.
7
The use of isotope effects to determine enzyme mechanisms.利用同位素效应来确定酶的作用机制。
Arch Biochem Biophys. 2005 Jan 1;433(1):2-12. doi: 10.1016/j.abb.2004.08.027.
8
Mechanistic and kinetic studies of inhibition of enzymes.酶抑制作用的机理和动力学研究
Cell Biochem Biophys. 2000;33(3):217-25. doi: 10.1385/cbb:33:3:217.
9
[Determination of kinetic constants in the general case of cooperative type or Michaelis enzymes inhibited by their substrate: theoretic analysis].[底物抑制的协同型或米氏酶一般情况下动力学常数的测定:理论分析]
C R Acad Sci III. 1986;303(12):495-500.
10
Inhibition and activation of enzymes. The effect of a modifier on the reaction rate and on kinetic parameters.酶的抑制与激活。修饰剂对反应速率及动力学参数的影响。
Acta Biochim Pol. 2000;47(1):233-57.

引用本文的文献

1
Identification of specialized metabolites from Artocarpus lacucha as potent α-glucosidase and acetylcholinesterase inhibitors: enzyme kinetic, in vitro and in silico study.从白桂木中鉴定出作为强效α-葡萄糖苷酶和乙酰胆碱酯酶抑制剂的特殊代谢产物:酶动力学、体外和计算机模拟研究
J Nat Med. 2025 May 6. doi: 10.1007/s11418-025-01904-8.
2
lipopeptides inhibit lipase activity and promote 3T3-L1 preadipocyte differentiation.脂肽抑制脂肪酶活性并促进 3T3-L1 前体脂肪细胞分化。
J Enzyme Inhib Med Chem. 2024 Dec;39(1):2417915. doi: 10.1080/14756366.2024.2417915. Epub 2024 Oct 21.
3
In Vitro In Silico Screening Strategy and Mechanism of Novel Tyrosinase Inhibitory Peptides from Nacre of .
珍珠层中新型酪氨酸酶抑制肽的体外计算机筛选策略及机制
Mar Drugs. 2024 Sep 15;22(9):420. doi: 10.3390/md22090420.
4
In Silico Identification and Molecular Mechanism of Novel Tyrosinase Inhibitory Peptides Derived from Nacre of .从珍珠层中鉴定新型酪氨酸酶抑制肽的计算与分子机制
Mar Drugs. 2024 Aug 7;22(8):359. doi: 10.3390/md22080359.
5
Regulation of Rubisco activity by interaction with chloroplast metabolites.Rubisco 活性通过与叶绿体代谢物的相互作用进行调节。
Biochem J. 2024 Aug 7;481(15):1043-1056. doi: 10.1042/BCJ20240209.
6
Prenylated flavonoids from inhibit mushroom tyrosinase activity and modulate melanogenesis in murine melanoma cells and zebrafish.来自[具体来源未提及]的异戊烯基黄酮可抑制蘑菇酪氨酸酶活性,并调节小鼠黑色素瘤细胞和斑马鱼中的黑色素生成。
Front Pharmacol. 2024 Jul 10;15:1422310. doi: 10.3389/fphar.2024.1422310. eCollection 2024.
7
A bacterial quorum sensing signal is a potent inhibitor of pyrimidine biosynthesis in the globally abundant .一种细菌群体感应信号是全球广泛存在的嘧啶生物合成的有效抑制剂。
Front Microbiol. 2023 Oct 6;14:1266972. doi: 10.3389/fmicb.2023.1266972. eCollection 2023.
8
Effects of Sodium Dodecyl Sulfate on the Enzyme Catalysis and Conformation of a Recombinant γ-Glutamyltranspeptidase from Bacillus licheniformis.十二烷基硫酸钠对来自地衣芽孢杆菌的重组γ-谷氨酰转肽酶的酶催化作用和构象的影响
Protein J. 2023 Feb;42(1):64-77. doi: 10.1007/s10930-023-10095-8. Epub 2023 Feb 4.
9
Itraconazole-Induced Increases in Gilteritinib Exposure Are Mediated by CYP3A and OATP1B.伊曲康唑引起的吉尔替尼暴露增加是由 CYP3A 和 OATP1B 介导的。
Molecules. 2022 Oct 12;27(20):6815. doi: 10.3390/molecules27206815.
10
A single amino acid transporter controls the uptake of priming-inducing beta-amino acids and the associated tradeoff between induced resistance and plant growth.一种单一的氨基酸转运蛋白控制着引发诱导β-氨基酸的摄取以及诱导抗性和植物生长之间的权衡。
Plant Cell. 2022 Nov 29;34(12):4840-4856. doi: 10.1093/plcell/koac271.