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I am asked to calculate the isocitrate lyase acticity in the original enzyme solutions, giving my results in micromoles of glyoxylate produced. min ^-1. mg protein ^-1

In my initial reaction protein assay was done on each of my THREE enzyme solutons that were obtained from seeds that had been soaked for :
                 ( Protein concentration)
24 hour   :  3.4  mg/ml
3 days    :   4.1 mg/ml
5 days    :   4.5 mg/ml

To measure the Isocitrate lyase acticity, to each of the three test tubes..1.5ml of various chemicals was added. Then 0.5 ml of the enzyme solution was added to each of three test tubes to get the reaction started. 10 minutes later 0.5 ml of a solution was added to stop the reaction.


Then: I had to make a standard solutionof both glyoxylate and alpha-ketogluterate into three seperate test tubes. Adding 1.5 ml of solutions to it and after incubation another 2ml of a different soltuion was added to give the sample colour. Their absorptions were measured. Then i took 1 ml of my ENZYME SOLUTION ( Initial experiment) and repeated the procedure described in this paragraph. ( Instead of glyox. and alpha, the 24 hour, 3 day and 5 day supernatant was added to 1.5 ml and then 2 ml of solutions)

I calculated the concentrations of the Alpha- glut. and Glyoxy. in the three experiment samples.
( I got concentrations of both alpha- ketogluterate. and glyoxylate for each of the three samples of 24 days , 3 days and 5 days)

 Now back to my initial questions....I am asked to calculate the isocitrate lyase acticity in the original enzyme solutions, giving my results in micromoles of glyoxylate produced. min ^-1. mg protein ^-1


Can someone help me to understand the link between the enzyme activity of the initial enzyme reaction and the concentration i found out from my standard solutions?

Thank you.

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No help needed. Figured it out. Thanks out to anyone who was considering helping.