Purification and properties of glutathione peroxidase from human placenta

Y. C. Awasthi, D. D. Dao, A. K. Lal, Satish Srivastava

Research output: Contribution to journalArticle

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Abstract

Glutathione peroxidase (glutathione-H2O2 oxidoreductase; EC 1.11.1.9) was purified to homogeneity from human placenta by using (NH4)2SO4 precipitation, ion-exchange chromatography, Sephadex gel filtration and preparative polyacrylamide-disc-gel electrophoresis. Glutathione peroxidase from human placenta is a tetramer, having 4g-atoms of selenium/mol of protein. The molecular weight of the enzyme is about 85,000 with a subunit size of about 22,000. Kinetic properties of the enzyme are described. On incubation with cyanide, glutathione peroxidase is completely and irreversibly inactivated and selenium is released as a low-molecular-weight fragment. Reduced glutathione, β-mercaptoethanol and dithiothreitol protect the enzyme from inactivation by cyanide and the release of selenium. Properties of human placental glutathione peroxidase are similar to those of isoenzyme A reported earlier by us from human erythrocytes. The presence of isoenzyme B, reported earlier by us in human erythrocytes, was not detected in placenta. Also selenium-independent glutathione peroxidase (isoenzyme II), which is specific for cumene hydroperoxide, was not present in human placenta.

Original languageEnglish (US)
Pages (from-to)471-476
Number of pages6
JournalBiochemical Journal
Volume177
Issue number2
StatePublished - 1979

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Glutathione Peroxidase
Placenta
Purification
Selenium
Isoenzymes
Cyanides
Glutathione
Enzymes
Molecular weight
Mercaptoethanol
Dithiothreitol
Chromatography
Erythrocytes
Molecular Weight
Electrophoresis
Disc Electrophoresis
Ion exchange
Oxidoreductases
Gels
Ion Exchange Chromatography

ASJC Scopus subject areas

  • Biochemistry

Cite this

Awasthi, Y. C., Dao, D. D., Lal, A. K., & Srivastava, S. (1979). Purification and properties of glutathione peroxidase from human placenta. Biochemical Journal, 177(2), 471-476.

Purification and properties of glutathione peroxidase from human placenta. / Awasthi, Y. C.; Dao, D. D.; Lal, A. K.; Srivastava, Satish.

In: Biochemical Journal, Vol. 177, No. 2, 1979, p. 471-476.

Research output: Contribution to journalArticle

Awasthi, YC, Dao, DD, Lal, AK & Srivastava, S 1979, 'Purification and properties of glutathione peroxidase from human placenta', Biochemical Journal, vol. 177, no. 2, pp. 471-476.
Awasthi YC, Dao DD, Lal AK, Srivastava S. Purification and properties of glutathione peroxidase from human placenta. Biochemical Journal. 1979;177(2):471-476.
Awasthi, Y. C. ; Dao, D. D. ; Lal, A. K. ; Srivastava, Satish. / Purification and properties of glutathione peroxidase from human placenta. In: Biochemical Journal. 1979 ; Vol. 177, No. 2. pp. 471-476.
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