Abstract
The rapid and specific determination of picomole quantities of δ-aminolevulinate has been accomplished by its specific enzymatic conversion to uroporphyrinogen I and fluorometric detection of the oxidized uroporphyrin I. The coupled enzyme assay was linear with time and protein concentration and required less than 3 h for 25 individual determinations. Under the standard assay conditions, 1 to 100 pmol of uroporphyrin I was reliably quantitated; these values corresponded to a range of ALA synthase activities from 0.15 to 15 nmol/h/ml of enzyme. The sensitivity of this method was comparable to the more time-consuming radiochemical determinations of ALA synthase. In addition, this method was at least 10 times more sensitive than the colorimetric assays for ALA synthase activity. The rapidity, specificity, and sensitivity of this new method make it useful for monitoring the purification of ALA synthase and for reliable determinations of low levels of ALA synthase activity in crude tissue or cultured cell homogenates.
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