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

@article{Loscalzo1986PurificationAC,
  title={Purification and characterization of human platelet glutathione-S-transferase.},
  author={Joseph Loscalzo and John D Freedman},
  journal={Blood},
  year={1986},
  volume={67 6},
  pages={1595-9}
}
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

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

Evolution of Enzyme Kinetic Mechanisms

Journal of Molecular Evolution • 2015
View 1 Excerpt

The antithrombotic effects of organic nitrates.

Trends in cardiovascular medicine • 1991
View 5 Excerpts

References

Publications referenced by this paper.
Showing 1-10 of 10 references

Ahokas iT: Inhibition of purified glutathione5-transferases by indomethacin

FA Nicholls
Biochem Biophys Res Commun • 1984

Is a slow-reacting substance-like compound involved in rat platelet aggregation

C Meringolo, G Bartolini, M Orlandi, V BarnaTomasi
Prostaglandins Med • 1979

Structure of leukotriene C. Identification of the amino acid part.

Biochemical and biophysical research communications • 1979

Glutathione-S-transferase-The first enzymatic step in mercapturic acid formation

WH Habig, Mi Pabst, WB iakoby
i Biol Chem • 1974

Chassequd LF: The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis

E Boyland
Adv Enzymol Rel Areas Mol Biol • 1969

Colorimetric Methods of Analysis, 3rd ed

FD Snell, CJ Snell
1949

Similar Papers

Loading similar papers…