You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data are obtained: [S] V0 -Inhibitor +Inhibitor 0.0001 33 17 0.0002 50 29 0.0005 71 50 0.001 83 67 0.002 91 80 0.005 96 91 0.01 98 95 0.02 99 98 0.05 100 99 0.1 100 100 0.2 100 100a) What is the Vmax in the absence of inhibitor? b) What is the Km in the absence of inhibitor? c) What is the Km in the presence of inhibitor? d) What kind of inhibitor is it likely to be?

Answer asap need to be answered by wednesday morning explain how a buffer works, using an ethanoic acid / sodium ethanoate system including how the system resists changes in ph upon addition of a small amount of base and upon addition of a small amount of acid respectively. include the following calculations in your i. calculate the ph of a solution made by mixing 25cm3 0.1m ch3cooh and 40cm3 0.1m ch3coo-na+. [ka = 1.74 x 10-5 m] ii. calculate the ph following the addition of a 10cm3 portion of 0.08 m naoh to 500cm3 of this buffer solution. iii. calculate the ph following the addition of a 10cm3 portion of 0.08 m hcl to 200cm3 of the original buffer solution.