Lineweaver- Burk Plot
In biochemistry, it is a graphical representation of the Lineweaver- Burk Plot equation of the ”enzyme kinetics” reported by “Hans Lineweaver” and ”Dean Burk” in 1934.
- However Vmax is triggered by at infinite substrate concentration. Moreover, it is not possible to find Vmax and Km from the hyperbolic slope.
- A difficulty was found in the equation, but later on ”The Michaelis-Menten equation” came forward and it was changed into an equation from a straight line by Lineweaver and Burk.
- It is also known as ”double reciprocal plot.”
- This equation is demonstrated by of Michaelis Menten equation which is represented a: Explanation:
”V” is the reaction velocity. Km is known as Michael Menten constant. Whereas, Vmax is the maximum reaction.[S] is the concentration of substrate.
- The graph gives us a straight line that crosses the y-axis. It is equal to 1/Vmax and the intercept on the x-axis is equal to Km/Vmax
- Furthermore, the constants Vmax and Km can be demonstrated experimentally. It can be measured accurately when Vo is measured at taking different substrate concentrations. Likewise, the double reciprocal of 1/Vo against 1/[S] is constructed thoroughly.
- There are two types of enzymes inhibitors. One is known as a competitive enzyme inhibitor while the other is known as a non-competitive enzyme inhibitor. These both can be differentiated through Lineweaver-Burk Plot
- This technique is very helpful in finding how an inhibitor binds to a particular enzyme.
- Competitive enzyme inhibitor can be known easily by Lineweaver- Burk Plot, if Vo is measured at different substrate concentrations in the presence of a very fixed and finite concentration of an inhibitor and vice versa.
- A competitive enzyme inhibitor generally booms and increases the slope of the Lineweaver-Burk plot. It usually changes the intercept on the x-axis, but generally, it leaves the intercept on the y-axis to remain unchanged barely.• Moreover, a non-competitive enzyme inhibitor can also be determined and can be known via the Lineweaver-Burk equation. It usually increases the slope of the experimental line, and it barely changes the intercept on the y-axis but leaves the intercept on the x-axis when remains unchanged.
Uses of Lineweaver-Burk Plot
- This equation is very helpful in determining the kinetics of the enzyme randomly in terms of Km and Vmax, wwhich is the constants present in the equation.
- It gives a quick visual suspicion of the different forms and shapes of enzyme inhibition.
• It gives more precision by linearizing the comparative data.