l-Dopa peroxidase activity of human erythrocyte catalase

Y. C. Awasthi, Satish Srivastava, L. M. Snyder, L. Edelstein, N. L. Fortier

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The human red cell hemolysate was found to have 3-(3′,4′-dihydroxyphenyl)-l-alanine (l-dopa) peroxidase activity. During the purification of glutathione peroxidase and catalase by ammonium sulfate precipitation, ion exchange chromatography, Sephadex gel filtration, and preparative polyacrylamide disc electrophoresis, the l-dopa peroxidase activity was found to be associated with catalase. Both sodium azide, 8 mM, and 3-amino-1,2,4-triazole, 50 mM, besides inhibiting catalase, inhibited the l-dopa peroxidase activity in each fraction. Ethylenediamine tetraacetic acid (EDTA), 4 mM, had no effect on catalase or l-dopa peroxidase activity, indicating that the oxidation of l-dopa is not a nonenzymatic process mediated by metal ions. Although the electrophoretic mobility of catalase, l-dopa peroxidase, and glutathione peroxidase are similar, a homogeneous preparation of glutathione peroxidase was free of l-dopa peroxidase activity. l-Dopa peroxidase in human red cells was co-purified with catalase.

Original languageEnglish (US)
Pages (from-to)763-769
Number of pages7
JournalThe Journal of Laboratory and Clinical Medicine
Volume89
Issue number4
StatePublished - 1977

Fingerprint

Dihydroxyphenylalanine
Human Activities
Catalase
Peroxidase
Erythrocytes
Glutathione Peroxidase
ethylenediamine
Cells
Amitrole
Disc Electrophoresis
Electrophoretic mobility
Sodium Azide
Ion Exchange Chromatography
Ammonium Sulfate
Chromatography
Electrophoresis
Alanine
Purification
Gel Chromatography
Metal ions

ASJC Scopus subject areas

  • Medicine(all)
  • Pathology and Forensic Medicine

Cite this

Awasthi, Y. C., Srivastava, S., Snyder, L. M., Edelstein, L., & Fortier, N. L. (1977). l-Dopa peroxidase activity of human erythrocyte catalase. The Journal of Laboratory and Clinical Medicine, 89(4), 763-769.

l-Dopa peroxidase activity of human erythrocyte catalase. / Awasthi, Y. C.; Srivastava, Satish; Snyder, L. M.; Edelstein, L.; Fortier, N. L.

In: The Journal of Laboratory and Clinical Medicine, Vol. 89, No. 4, 1977, p. 763-769.

Research output: Contribution to journalArticle

Awasthi, YC, Srivastava, S, Snyder, LM, Edelstein, L & Fortier, NL 1977, 'l-Dopa peroxidase activity of human erythrocyte catalase', The Journal of Laboratory and Clinical Medicine, vol. 89, no. 4, pp. 763-769.
Awasthi YC, Srivastava S, Snyder LM, Edelstein L, Fortier NL. l-Dopa peroxidase activity of human erythrocyte catalase. The Journal of Laboratory and Clinical Medicine. 1977;89(4):763-769.
Awasthi, Y. C. ; Srivastava, Satish ; Snyder, L. M. ; Edelstein, L. ; Fortier, N. L. / l-Dopa peroxidase activity of human erythrocyte catalase. In: The Journal of Laboratory and Clinical Medicine. 1977 ; Vol. 89, No. 4. pp. 763-769.
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AU - Awasthi, Y. C.

AU - Srivastava, Satish

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AU - Fortier, N. L.

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N2 - The human red cell hemolysate was found to have 3-(3′,4′-dihydroxyphenyl)-l-alanine (l-dopa) peroxidase activity. During the purification of glutathione peroxidase and catalase by ammonium sulfate precipitation, ion exchange chromatography, Sephadex gel filtration, and preparative polyacrylamide disc electrophoresis, the l-dopa peroxidase activity was found to be associated with catalase. Both sodium azide, 8 mM, and 3-amino-1,2,4-triazole, 50 mM, besides inhibiting catalase, inhibited the l-dopa peroxidase activity in each fraction. Ethylenediamine tetraacetic acid (EDTA), 4 mM, had no effect on catalase or l-dopa peroxidase activity, indicating that the oxidation of l-dopa is not a nonenzymatic process mediated by metal ions. Although the electrophoretic mobility of catalase, l-dopa peroxidase, and glutathione peroxidase are similar, a homogeneous preparation of glutathione peroxidase was free of l-dopa peroxidase activity. l-Dopa peroxidase in human red cells was co-purified with catalase.

AB - The human red cell hemolysate was found to have 3-(3′,4′-dihydroxyphenyl)-l-alanine (l-dopa) peroxidase activity. During the purification of glutathione peroxidase and catalase by ammonium sulfate precipitation, ion exchange chromatography, Sephadex gel filtration, and preparative polyacrylamide disc electrophoresis, the l-dopa peroxidase activity was found to be associated with catalase. Both sodium azide, 8 mM, and 3-amino-1,2,4-triazole, 50 mM, besides inhibiting catalase, inhibited the l-dopa peroxidase activity in each fraction. Ethylenediamine tetraacetic acid (EDTA), 4 mM, had no effect on catalase or l-dopa peroxidase activity, indicating that the oxidation of l-dopa is not a nonenzymatic process mediated by metal ions. Although the electrophoretic mobility of catalase, l-dopa peroxidase, and glutathione peroxidase are similar, a homogeneous preparation of glutathione peroxidase was free of l-dopa peroxidase activity. l-Dopa peroxidase in human red cells was co-purified with catalase.

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