Abstract
The glyoxalase activity of aerated mammalian erythrocytes is increased by plasma in low concentrations, by glucose, by adenosine and inosine and by bovine albumin. Glucosamine and sodium arsenate, on the other hand, produce a fall in glyoxalase activity. In all instances except that of albumin, a corresponding alteration of reduced glutathione level was produced by the addition of each of these materials. Plasma and serum albumin in high concentrations produce, under the conditions employed, a decrease in glyoxalase activity which is overcome by the further addition of methyl-glyoxal, suggesting that the fall in activity is due to a decrease in substrate concentration.