Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes.

No abstract is available for this paper.

• Publication year

  1996

• Venue

  Blood

• Publication date

  1996-02-15

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1182/BLOOD.V87.4.1595.BLOODJOURNAL8741595PMID 8608252
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• [Glutathione peroxidase].

  1995cited by this paper
• Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes.

  1994cited by this paper
• Decreased catalase activity is the underlying mechanism of oxidant susceptibility in glucose-6-phosphate dehydrogenase-deficient erythrocytes.

  1993cited by this paper
• NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes.

  1991cited by this paper
• Erythrocyte defense against hydrogen peroxide: preeminent importance of catalase.

  1991cited by this paper
• Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes.

  1989cited by this paper
• The function of catalase-bound NADPH.

  1987cited by this paper
• Erythrocyte catalase. A somatic oxidant defense?

  1986cited by this paper
• Regulation of glucose-6-phosphate dehydrogenase in human erythrocytes.

  1986cited by this paper
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  1984cited by this paper
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  1984cited by this paper
• Catalase in vitro.

  1984cited by this paper
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  1976cited by this paper
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  1974cited by this paper
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