Lineweaver-burk Plot

Enzyme Activity Analysis Substrate-Velocity Curves and ...

Creating a Lineweaver-Burk Plot Transforming the Data From the Results sheet Baseline-corrected of Substrate-velocity data , click Analyze . Select Transforms from the Data manipulations analysis list.

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Using Microsoft Excel to Plot and Analyze Kinetic Data

By creating a double-reciprocal plot (or Lineweaver-Burk plot) the values m max for K and V can be determined from a regression line through the values for 1/S vs. 1/v.

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Lineweaver-Burke Problems

Lineweaver-Burk Problems 1) The initial rate for an enzyme catalyzed reaction has been determined at a number of substrate concentrations. Data are as follows [S] (umoles/L) V (umoles/L/min) 5 22 10 39 20 65 50 102 100 120 200 135 a) Use a Lineweaver-Burk plot (1/[S] vs 1/V) to determine Vmax ...

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Using Microsoft Excel to Plot and Analyze Kinetic Data

Three plots were ® produced from each assay, one representing the Michaelis-Menton equation and the other two representing linearized forms of that equation, specifically a double-reciprocal plot called a Lineweaver-Burk plot and an m max Eadie-Hofstee plot.

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Cheryl Coolidge

The Lineweaver Burk "double reciprocal" plot allows for analysis of enzymatic data when V max has not been clearly reached. The derivation is as follows:

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Chem*2580 Lecture 15 Experimental Enzyme Kinetics: Linear Plots

The result is known as the Lineweaver-Burk plot, or Double Reciprocal plot - 1 / K M 1 / V max K M / V max 1 / [S] 1 / v o x-intercept y-intercept slope X-axis Y-axis The Lineweaver-Burk plot is usually extrapolated to the negative x -axis.

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Sample questions from old Exam III – Spring 2011 BCHS 3304 ...

Lineweaver-Burk plot to answer the following questions. 11. What is the KM of the Winease reaction? A. 10 μM B. 0.33 mM C. 0.1 μM D. 0.1 mM

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Lecture 12 Enzymes: Inhibition

• Given a Lineweaver-Burk plot (1/V o vs. 1/[S]) , find/calculate V max and K m from the graph. Learning Objectives, continued •Explain competitive, uncompetitive, and pure noncompetitive inhibition in terms of a diagram of linked reaction equilibria for formation of ES, EI, and (if it can form) EIS.

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BCMB 3100 -Chapter 5 Lecture

BCMB 3100 -Chapter 5 Lecture • Enzymes • Six Classes (IUBMB) • Kinetics • Michaelis-Menten Equation • Vo, Km, Vmax, Kcat • Lineweaver-Burk Plot Principles of Kinetics (for non-enzyme-catalyzed reactions) (1) first -order reaction k S  P  [P]= v = k[S] rate equation  t v = velocity ...

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The Kinetics of Enzyme Reactions

How close were your estimates to the values from the Lineweaver-Burk plot? 2. How does the concentration of an inhibitor, (I), for competitive inhibition influence: 1) the v o as a function of (S) ; and 2) the Lineweaver-Burk plot?

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