A report was presented concerning the usefulness of glucose-6- phosphate-dehydrogenase (G6PD) as a macromolecular marker of acrolein (107028) exposure. Studies have shown that acrolein inactivated G6PD in-vitro. This occurred in purified enzyme (Torula yeast), enzyme partially purified from human erythrocytes, and in human erythrocytes with subsequent isolation of G6PD. Between 30 and 60 minutes at room temperature the inactivation was between 60% and 80% complete. The results indicated a dose dependent inactivation of the erythrocyte G6PD in-situ or as a purified enzyme from human erythrocytes or yeast. Amino acid analysis on the chemically modified yeast G6PD demonstrated a formation of a lysine adduct which the authors suggest is probably linked to the inactivation. The authors conclude that this assay may serve as a useful biomonitor as it provides a direct measure of enzymatic activity, it is a simple, accurate assay and furthermore, the human red blood cell, with a lifetime of about 120 days, would provide G6PD with 120 days of exposure to low doses of acrolein and essentially perform as an integrated dose monitor. The system, therefore, offers an advantage over serum proteins which possess shorter half-lives.
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