Research Article| Volume 63, ISSUE 1, P106-121, January 1964

Hemolytic effect of primaquine. XVI. Glyoxalase activity of primaquine-sensitive and normal erythrocytes

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      The activity of the sulfhydryl-dependent enzyme, glyoxalase, has been measured in primaquine-sensitive (G-6-PD deficient) and in normal (nonsensitive) erythrocytes by a technique that permits assay of the activity of the enzyme both in hemolysates and in whole (intact) cells. The mean glyoxalase activity of hemolysates of red cells from primaquine-sensitive Negro subjects was slightly but significantly higher than the mean activity in hemolysates of red cells from normal subjects. The glyoxalase activity of whole cells was not significantly different in the 2 groups. The elevated glyoxalase activity in hemolysates of primaquine-sensitive erythrocytes cannot be explained by their younger mean cell age. During administration of the hemolytic drug, primaquine, to sensitive individuals, the glyoxalase activity of the whole cells decreased coincident with a fall in the levels of reduced glutathione. The glyoxalase activity in hemolysates did not consistently reflect the enzyme activity as measured in whole cells. The glyoxalase activity of the erythrocytes of primaquine-sensitive subjects increased during the reticulocytosis following drug-induced hemolytic anemia but did not increase in erythrocytes of either sensitive or normal individuals during the reticulocytosis following acute phlebotomy. The glyoxalase activity apparently is elevated in young erythrocytes only in certain conditions, and then only under specific types of stress.
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