Purification and characterization of human platelet glutathione-S-transferase.

  title={Purification and characterization of human platelet glutathione-S-transferase.},
  author={Joseph Loscalzo and John D Freedman},
  volume={67 6},
A glutathione-S-transferase was isolated and purified to homogeneity from human platelets. With a combination of ammonium sulfate fractionation and chromatographic methods, 0.2 mg of pure enzyme was obtained from 9 X 10(11) platelets with a 12% recovery. The purified enzyme had a specific activity of 7.5 U per milligram, representing an approximately 1,100-fold purification. The enzyme was found to be anionic, with an isoelectric point of 4.6. With reduced glutathione as a co-substrate… CONTINUE READING


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