posted by stew .
An enzyme sample contains 24 mg protein/mL. Of this sample, 20 microliters in a standard incubation volume of 0.1 mL catalyzed the incorporation of glucose into glcogen at a rate of 1.6 nmol/min. Of this sample, 50 mL were fractionated by ammonium sulfate precipitation. The fraction precipitating between 30 and 50% saturation was redissolved in a total volume of 10 mL and dialyzed. The solution after dialysis had 12 mL and contained 30 mg protein/mL. Of the purified fraction, 20 microliters catalyzed the reaction rate of 5.9 nmol/min under the standard assay conditions. calculate the following:
A. The recovery of enzyme after the ammonium sulfate step.
B. The fold purification after the ammonium sulfate step.
by the way, this question is different from the previous question i asked.