No abstract

A homogenate of guinea pig polymorphonuclear leucocytes contains an enzyme system capable of oxidizing, in presence of oxygen, NADPH and NADH with the formation of hydrogen peroxide. The enzyme is much more active towards NADPH than to NADH. The presence of manganese ions strongly enhances the oxidase activity. It is suggested that the release of the NADPH oxidase in the leucocytes, during phagocytosis, accounts for the stimulation of the hexose monophosphate pathway that occurs in phagocytosis.

No abstract

A homogenate of guinea pig polymorphonuclear leucocytes contains an enzyme system capable of oxidizing, in presence of oxygen, NADPH and NADH with the formation of hydrogen peroxide. The enzyme is much more active towards NADPH than to NADH. The presence of manganese ions strongly enhances the oxidase activity. It is suggested that the release of the NADPH oxidase in the leucocytes, during phagocytosis, accounts for the stimulation of the hexose monophosphate pathway that occurs in phagocytosis.

Erythrocytes from normal subjects and from cases of iron deficiency anemia were exposed to hydrogen peroxide and the extent of membrane lipid peroxidation studied. Significantly less peroxidation was observed in intact anemic erythrocytes compared to normal. However, when isolated membrane lipids were subjected to peroxidation, there was no significant difference between the two groups. It is unlikely that lipid peroxidation per se plays a major role in the reported decrease in red cell life-span in iron deficiency.