Some properties of human erythrocyte pyrimidine 5'-nucleotidase.

In haemolysates human erythrocyte pyrimidine 5'-nucleotidase had a single optimum at pH 7.2 with CMP and 6.75 with UMP as substrate. The purified enzyme showed two pH optima at pH 6.25 and 7.2 with UMP as substrate. The enzyme was inhibited by both its products - inorganic phosphate and pyrimidine nucleoside. The inhibition by inorganic phosphate appeared to be non-competitive with Ki = 1.5 mM. Contrary to previous reports adenosine and inosine did not inhibit the enzyme.