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If an enzyme sample contains 24 mg protein/ml of this sample, 20 micro liters in a standard incubation volume of 0.1 mL catalyzed the incorporation of glucose into glycogen at a rate of 1.6 nmol/min. Of this sample, 50mL were fractionated by ammonium sulfate precipitation. The fraction precipitating between30 and 50% saturation was redissolved in a total volume of 10 ml and dialyzed. The solution after dialysis had 12mL and contained30 mg protein/mL. Of the purified fraction, 20 micro liters catalyzed the reaction rate of 5.9 nmol/min under the standard assay conditions. Compute the following:
A. State the recovery of enzyme after the ammonium sulfate step.B. State the fold purification after the ammonium sulfate step.
Show all the steps in the mechanism for the following reaction, When benzene is mixed with deuterated sulfuric acid, deuterium is slowly incorporated onto the ring. Show the mechanism for this reaction and explain how this relates the sulfonation of ..
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