Kinetic and electrophoretic studies of human erythrocytes deficient in pyrimidine 5'-nucleotidase.
The mutant enzyme of a patient with hereditary pyrimidine 5'-nucleotidase deficiency was analyzed biochemically. Partially purified by DEAE-Sephadex and concentrated by ultrafiltration, the enzyme had a high Km for the substrate uridine monophosphate. Utilization of the substrate cytidine monophosphate was normal, but utilization of adenosine monophosphate was greatly increased. The enzyme was stable to heat; the pH optimum was acidic. Electrophoresis of the enzyme revealed a very faint, slower than normal band.
D000328:Adult; D002852:Chromatography, Ion Exchange / Q000379:methods; D004592:Electrophoresis, Starch Gel / Q000379:methods; D004912:Erythrocytes / Q000201:enzymology*; D005260:Female; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009699:N-Glycosyl Hydrolases / Q000032:analysis / Q000172:deficiency*
D009699:N-Glycosyl Hydrolases