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Human erythrocyte pyrimidine 5'-nucleotidase (P5N) was separated into two subclasses. P5N-I and P5N-II, by DEAE Bio-Gel A column chromatography. Their enzymological properties were studied using five normal subjects and five patients with different P5N deficiencies. Study of the normal subjects showed that P5N-I and P5N-II have distinctive properties, and P5N-II is similar to the 5'-nucleotidase in rat liver cytosol. The P5N-II from the five subjects with this deficiency had normal activity and other normal enzymological properties. However, the P5N-I from these patients had abnormal properties, including reduced activity. These variant enzymes had a high Michaelis constant for substrate cytidine 5'-monophosphate and were heat stable. The optimum pH was shifted towards the acidic side in two patients, towards the basic side in one, and was unchanged in the other two. These results strongly suggest that the main cause of P5N deficiency is an abnormality of P5N-I, probably arising from a structural gene mutation.
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