The presence of NADPH‐glyceraldehyde 3‐phosphate oxidoreductase in macrophages

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Abstract
The existence of an NADPH‐oxidoreductase which utilizes D‐glyceraldehyde 3‐phosphate as substrate has been demonstrated in mouse peritoneal macrophages. D‐Glyceraldehyde could also serve as substrate, albeit with a 10‐fold lower efficiency. No NADH oxidation could be demonstrated with either substrate. Addition of D‐glyceraldehyde to cultured macrophages increased the rate of activity of the hexose monophosphate shunt to about 65% of the level observed i zymosan A‐stimulated macrophages. The possible involvement of the oxidoreductase in this phenomenon and in the inhibitory effect of D‐glyceraldehyde on the production of oxygen free radicals by zymosan‐stimulated cells is discussed.