Contents
How do you find Km and Vmax from a Lineweaver-Burk plot?
Ease of Calculating the Vmax in Lineweaver-Burk Plot Next, you will obtain the rate of enzyme activity as 1/Vo = Km/Vmax (1/[S]) + 1/Vmax, where Vo is the initial rate, Km is the dissociation constant between the substrate and the enzyme, Vmax is the maximum rate, and S is the concentration of the substrate.
What is km in Lineweaver-Burk plot?
The y-intercept of the Lineweaver- Burk plot is the reciprocal of maximum velocity. KM: Michaelis-Menten constant or enzyme affinity. The lower the KM the higher the affinity. Graphically the x-intercept of the line is -1/KM. Kcat: turnover number, or reactions per unit time.
How do you find km from Vmax?
From the graph find the maximum velocity and half it i.e. Vmax/2. Draw a horizontal line from this point till you find the point on the graph that corresponds to it and read off the substrate concentration at that point. This will give the value of Km.
Is Michaelis Menten vs Lineweaver-Burk more accurate?
For instance; Lineweaver-Burke plot, the most favoured plot by researchers, has two distinct advantages over the Michaelis-Menten plot, in that it gives a more accurate estimate of Vmax and more accurate information about inhibition. It increases the precision by linearizing the data.
What is the purpose of a Lineweaver-Burk plot?
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.
What are the units of Km and Vmax?
KM is a the concentration substrate required to approach the maximum reaction velocity – if [S]>>Km then Vo will be close to Vmax. KM is a concentration. It will have units of: (M),or ( M),etc. liter liter KM depends only on the structure of the enzyme and is independent of enzyme concentration.
How to find km and Vmax from a Lineweaver Burk plot?
The double-reciprocal (also known as the Lineweaver-Burk) plot is created by plotting the inverse initial velocity (1/V0) as a function of the inverse of the substrate concentration (1/ [S]). The Vmax can be accurately determined and thus KM can also be determined with accuracy because a straight line is formed. What is the unit of KM?
How to calculate enzyme activity in Lineweaver Burk plot?
Ease of Calculating the Vmax in Lineweaver-Burk Plot Next, you will obtain the rate of enzyme activity as 1/Vo = Km/Vmax (1/ [S]) + 1/Vmax, where Vo is the initial rate, Km is the dissociation constant between the substrate and the enzyme, Vmax is the maximum rate, and S is the concentration of the substrate. Beside above, what is the unit of KM?
How is the slope of a Lineweaver-Burk plot determined?
Competitive inhibition can be recognized by using a Lineweaver–Burk plot if V 0 is measured at different substrate concentrations in the presence of a fixed concentration of inhibitor. A competitive inhibitor increases the slope of the line on the Lineweaver–Burk plot, and alters the intercept on the x-axis (since Km is increased), but …
Who is the author of the Lineweaver-Burk plot?
Lineweaver–Burk Plot. The 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. Lineweaver–Burk Plot.