Purification and characterization of activated human erythrocyte prolidase.

@article{Richter1989PurificationAC,
  title={Purification and characterization of activated human erythrocyte prolidase.},
  author={Andrea M. Richter and Gerald Lancaster and Francis Y. M. Choy and Peter Hechtman},
  journal={Biochemistry and cell biology = Biochimie et biologie cellulaire},
  year={1989},
  volume={67 1},
  pages={34-41}
}
Prolidase (E.C. 3.4.13.9) has been purified 7500-fold to homogeneity from human erythrocytes in a Mn2+-activated form using conventional and fast protein liquid chromatography columns. The procedure includes a 1-h incubation of the crude hemolysate at 50 degrees C with 1 mM MnCl2. Following this novel step, prolidase retains full activity, obviating the requirement for preincubation of each enzyme fraction with Mn2+ prior to assay. Preincubation with MnCl2 does not change the isoelectric point… CONTINUE READING
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