The enzymatic destruction of oxidizing products produced during metabolic reduction of oxygen in the cell (such as singlet oxygen, H2O2 and OH radical) involves the concerted action of superoxide dismutase-which removes O2 - and yields H2O2-and H2O2 removing enzymes such as catalase and glutathione peroxidase. A difference in distribution or ratio of these enzymes in various tissues may result in a different reactivity of oxygen radicals. It was found that in red blood cells superoxide dismutase and catalase are extracted in the same fraction as hemoglobin, while glutathione peroxidase appears to be "loosely" bound to the cellular structure. This suggests that in red blood cells catalase acts in series with superoxide dismutase against bursts of oxygen radicals formed from oxyhemoglobin, while glutathione & peroxidase may protect the cell membrane against low concentrations of H2O2. On the other hand, catalase activity is absent in various types of ascites tumor cells, while glutathione peroxidase and superoxide dismutase are found in the cytoplasm. However, the peroxidase/dismutase ratio is lower than in liver cells, and this may provide an explanation for the higher susceptibility of tumor cells to treatments likely to involve oxygen radicals. © 1976 Dr. W. Junk b.v. Publishers.

Enzyme defense against reactive oxygen derivatives. II. Erythrocytes and tumor cells / Bozzi, Argante; Irene, Mavelli; Alessandro Finazzi, Agro; Strom, Roberto; Anna Maria, Wolf; Bruno, Mondovi; Giuseppe, Rotilio. - In: MOLECULAR AND CELLULAR BIOCHEMISTRY. - ISSN 0300-8177. - STAMPA. - 10:1(1976), pp. 11-16. [10.1007/bf01731676]

Enzyme defense against reactive oxygen derivatives. II. Erythrocytes and tumor cells

BOZZI, Argante;STROM, Roberto;
1976

Abstract

The enzymatic destruction of oxidizing products produced during metabolic reduction of oxygen in the cell (such as singlet oxygen, H2O2 and OH radical) involves the concerted action of superoxide dismutase-which removes O2 - and yields H2O2-and H2O2 removing enzymes such as catalase and glutathione peroxidase. A difference in distribution or ratio of these enzymes in various tissues may result in a different reactivity of oxygen radicals. It was found that in red blood cells superoxide dismutase and catalase are extracted in the same fraction as hemoglobin, while glutathione peroxidase appears to be "loosely" bound to the cellular structure. This suggests that in red blood cells catalase acts in series with superoxide dismutase against bursts of oxygen radicals formed from oxyhemoglobin, while glutathione & peroxidase may protect the cell membrane against low concentrations of H2O2. On the other hand, catalase activity is absent in various types of ascites tumor cells, while glutathione peroxidase and superoxide dismutase are found in the cytoplasm. However, the peroxidase/dismutase ratio is lower than in liver cells, and this may provide an explanation for the higher susceptibility of tumor cells to treatments likely to involve oxygen radicals. © 1976 Dr. W. Junk b.v. Publishers.
1976
catalase; glutathione peroxidase; reactive oxygen species; superoxide dismutase
01 Pubblicazione su rivista::01a Articolo in rivista
Enzyme defense against reactive oxygen derivatives. II. Erythrocytes and tumor cells / Bozzi, Argante; Irene, Mavelli; Alessandro Finazzi, Agro; Strom, Roberto; Anna Maria, Wolf; Bruno, Mondovi; Giuseppe, Rotilio. - In: MOLECULAR AND CELLULAR BIOCHEMISTRY. - ISSN 0300-8177. - STAMPA. - 10:1(1976), pp. 11-16. [10.1007/bf01731676]
File allegati a questo prodotto
Non ci sono file associati a questo prodotto.

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/477687
 Attenzione

Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo

Citazioni
  • ???jsp.display-item.citation.pmc??? 6
  • Scopus 92
  • ???jsp.display-item.citation.isi??? ND
social impact