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.

faculty.weber.edu

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:

www.colby-sawyer.edu

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.

www.comp.nus.edu.sg

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

bchs.uh.edu

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.

www.biochem.arizona.edu

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 ...

www.ccrc.uga.edu

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?

academic.pgcc.edu

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