ラインウィーバー・バークの式
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- the act of regarding as equal (同)equating
- a mathematical statement that two expressions are equal
- United States frontierswoman and legendary figure of the Wild West noted for her marksmanship (1852-1903) (同)Martha Jane Burk, Burke, Martha Jane Burke, Calamity Jane
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- 等式; 方程式
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/26 10:47:58」(JST)
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An example of a Lineweaver-Burke plot.
In biochemistry, the Lineweaver–Burk plot (or double reciprocal plot) is a graphical representation of the Lineweaver–Burk equation of enzyme kinetics, described by Hans Lineweaver and Dean Burk in 1934.[1]
Contents
- 1 Derivation
- 2 Use
- 3 Problems with the method
- 4 See also
- 5 References
- 6 External links
Derivation
The plot provides a useful graphical method for analysis of the Michaelis–Menten equation:
Taking the reciprocal gives
where V is the reaction velocity (the reaction rate), Km is the Michaelis–Menten constant, Vmax is the maximum reaction velocity, and [S] is the substrate concentration.
Use
Lineweaver–Burk plots of different types of reversible enzyme inhibitors. The arrow shows the effect of increasing concentrations of inhibitor.
The Lineweaver–Burk plot was widely used to determine important terms in enzyme kinetics, such as Km and Vmax, before the wide availability of powerful computers and non-linear regression software. The y-intercept of such a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents −1/Km. It also gives a quick, visual impression of the different forms of enzyme inhibition.
The double reciprocal plot distorts the error structure of the data, and it is therefore unreliable for the determination of enzyme kinetic parameters. Although it is still used for representation of kinetic data,[2] non-linear regression or alternative linear forms of the Michaelis–Menten equation such as the Hanes-Woolf plot or Eadie–Hofstee plot are generally used for the calculation of parameters.[3]
When used for determining the type of enzyme inhibition, the Lineweaver–Burk plot can distinguish competitive, non-competitive and uncompetitive inhibitors. Competitive inhibitors have the same y-intercept as uninhibited enzyme (since Vmax is unaffected by competitive inhibitors the inverse of Vmax also doesn't change) but there are different slopes and x-intercepts between the two data sets. Non-competitive inhibition produces plots with the same x-intercept as uninhibited enzyme (Km is unaffected) but different slopes and y-intercepts. Uncompetitive inhibition causes different intercepts on both the y- and x-axes .
Problems with the method
The Lineweaver–Burk plot is classically used in older texts, but is prone to error, as the y-axis takes the reciprocal of the rate of reaction – in turn increasing any small errors in measurement. Also, most points on the plot are found far to the right of the y-axis (due to limiting solubility not allowing for large values of [S] and hence no small values for 1/[S]), calling for a large extrapolation back to obtain x- and y-intercepts.[4]
See also
- Michaelis–Menten kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
References
- ^ Lineweaver, H and Burk, D. (1934). "The Determination of Enzyme Dissociation Constants". Journal of the American Chemical Society 56 (3): 658–666. doi:10.1021/ja01318a036.
- ^ Hayakawa, K.; Guo, L.; Terentyeva, E.A.; Li, X.K.; Kimura, H.; Hirano, M.; Yoshikawa, K.; Nagamine, T. et al. (2006). "Determination of specific activities and kinetic constants of biotinidase and lipoamidase in LEW rat and Lactobacillus casei (Shirota)". J Chromatogr B Analyt Technol Biomed Life Sci 844 (2): 240–50. doi:10.1016/j.jchromb.2006.07.006. PMID 16876490.
- ^ Greco, W. R. and Hakala, M. T., (1979). "Evaluation of methods for estimating the dissociation constant of tight binding enzyme inhibitors," (PDF). J. Biol. Chem. 254 (23): 12104–12109. PMID 500698.
- ^ Dowd, John E.; Riggs, Douglas S. (1965). "A Comparison of Estimates of Michaelis–Menten Kinetic Constants from Various Linear Transformations". J. Biol. Chem 240 (2): 863–869.
External links
- NIH guide, enzyme assay development and analysis
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Proteins: enzymes
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
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- 15-18
- 2.1
- 3.1
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- 5.1
- 6.1-3
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UpToDate Contents
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English Journal
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- Pakistan journal of biological sciences: PJBS.Pak J Biol Sci.2014 Jan 15;17(2):277-81.
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- Usefulness and accuracy of the international normalized ratio and activity percent of prothrombin time in patients with liver disease.
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- AIM: In order to determine the most reliable reporting style for prothrombin time (PT) in patients with liver disease, we examined the correlations between the plasma antigen levels of clotting factors and the PT activity percent or two international normalized ratios (INR), and compared the inter-r
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Japanese Journal
- Inhibitory Effect of High Concentrations of Ferric Ions on the Activity of Acidithiobacillus ferrooxidans
- Kawabe Yoshishige,Inoue Chihiro,Suto Koichi [他],CHIDA TADASHI
- Journal of bioscience and bioengineering 96(4), 375-379, 2003-10-25
- … Lineweaver-Burk plots revealed typical competitive inhibition kinetics, because the slopes varied with the ferric ion concentration. … The kinetic equation based on this inhibition model agreed with the experimental observation at a high ferric ion concentration where the bacterium is usually exposed in bioleaching and biooxidation plants. …
- NAID 110002665209
- 硫酸化シクロデキストリンを用いるキャピラリー電気泳動による光学異性体の分離
- 桑原 由佳里,泉本 真一,西 博行
- 分析化学 50(1), 69-77, 2001-01-05
- キャピラリー電気泳動は光学異性体の分離に優れており, シクロデキストリンをはじめとした, 多くの光学活性化合物がキラルセレクターとして応用されている。特に, 電荷を持つシクロデキストリンは光学認識能に優れ, 多様な薬物の光学異性体分離が報告されている. 硫酸化シクロデキストリンも幅広い光学認識能を持つことが知られているが, 従来のものはβ型のみ利用可能で, しかも硫酸基の導入数が低いものであった. …
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- Reliability of Various Methods of Determining Enzyme Kinetics Parameters
- 山舘 周恒,関口 光夫,太田 好次,長村 洋一,河野 均也,石黒 伊三雄
- Japanese Journal of Clinical Chemistry 26(1), 31-37, 1997
- … The Lineweaver-Burk plot or Hanes-Woolf plot is usually used to determine enzyme kinetics parameters, such as K<SUB>m</SUB>, in one-substrate reaction. … The reliability of the enzyme kinetics parameters in two-substrate reactions determined by the simplified method was evaluated using the optimized reaction rates equation calculated by a computer program "ASNOP". …
- NAID 130003357458
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