Uroporphyrinogen Decarboxylase

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Abstract
A method for measuring the activity of uroporphyrinogen decarboxylase from a variety of sources is described. Porphyrinogen substrates are generated by enzymic synthesis or chemical reduction. Substrates and enzyme are incubated under standardized conditions. The reactions are then stopped and the reaction products, as well as unmetabolized substrate, are absorbed on talc, eluted and esterified. Porphyrin esters are then separated and quantified using high performance liquid chromatography. [The method is applied to the measurement of the enzyme activity in rat liver, normal human erythrocytes and erythrocytes from patients with porphyria cutanea tarda.].