Clinical Chemistry
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Clinical Chemistry 38: 584-588, 1992;
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Clinical Chemistry, Vol 38, 584-588, Copyright © 1992 by American Association for Clinical Chemistry

Optimized spectrophotometric determination of aldehyde dehydrogenase activity in erythrocytes

RD Johnson, J Bahnisch, B Stewart, DJ Shearman and JB Edwards
Department of Medicine, University of Adelaide, South Australia.

We describe a reliable and sensitive semiautomated spectrophotometric assay of aldehyde dehydrogenase (ALDH; EC 1.2.1.3) activity in erythrocytes. The hemolysate can be stabilized with sucrose, and the technique involves only microliters of hemolysate on a centrifugal analyzer. The use of microcolumns to remove interfering hemoglobin is avoided, and reproducibility of the assay has been improved by manipulating the inherent lactate dehydrogenase activity of erythrocytes by adding lactate and oxalate to the reaction mixture. These modifications have decreased the analytical imprecision of the assay, allowing a better appraisal of aldehyde dehydrogenase activity in erythrocytes as a biological marker of excess alcohol consumption. Erythrocytic ALDH activity was significantly less in 40 alcoholics than in 145 teetotallers (median activity 128 vs 219 mU/g of hemoglobin, respectively; P = 0.0001), indicating the potential of this assay as a useful marker of excess alcohol consumption.


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N. K. HANSELL, D. PANG, A. C. HEATH, N. G. MARTIN, and J. B. WHITFIELD
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P. A. Dockham, L. Sreerama, and N. E. Sladek
Relative Contribution of Human Erythrocyte Aldehyde Dehydrogenase to the Systemic Detoxification of the Oxazaphosphorines
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