21. This image of 'Lineweaver Burk plot' is mentioning a reciprocal plot of V and [S] i.e. 1/V and 1/[S].
And, according to Lineweaver Burk plot,
1/V= Km/Vmax.1/[S] +1/Vmax
Following this equation,
the point where the straight line touches the X axis is negative value of 1/Km (-1/Km).
24. The approximate Km for the control (No [l]) is
-1/Km= -5 mM Or, Km=2mM
22. Approximate Vmax for 4mM Km value will be
1/Vmax= Y intercept which is near to 1/V=3mM/min or V=1/4 mM/min i.e. 0.25mM/min
24. The KI values are 0.5mM
QUESTION 21 Consider the following graph and answer questions 21 through 24 below: 10 Calen 02...
QUESTION 21 Consider the following graph and answer questions 21 through 24 below: 10 Cat N-2 1/v(min/mm) -5 - 1 0 1 2 3 4 5 6 1/[S] (mM1) TI QUESTION 22 What is the approximate Vmax for [1] = 4 mM? OA. 0.25 uM/min, OB.0.50 MM/min, OC.2.00 uM/min, OD.3.00 uM/min, OE. 4.00 uM/min, F. None of the above. What type inhibitor is I? A.competitive, B.uncompetitive, C.pure-noncompetitive, OD. mixed ( K'j > Ki), O E. all of the above, OF....
what is the approximage Vmax for [I]=4mM what type of inhibitor is I? 10 Ilv(min MM) 1/[S] (mm) 24. What is the approximate Km for the Control (No [U)? OA. -3.3 MM OB.-2.5 mm, OC.5 mM OD.3.3 mm, O E.0.2 mm, OF. none of the above.
Scatchard analysis may give information about? O A. the ligand binding constant (Kb) of a protein, OB. the number of ligand binding sites on a protein, the type of homotropic cooperativity with ligand binding, OD. Bmax: O E. all of the above, OF. none of the above. In glycolysis, fructose 1,6-bisphosphate is converted to two products with a AG'º of 23.8 kJ/mol. Under what conditions encountered in a normal cell will the free-energy change (AG) be negative, enabling the reaction...