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Science 19 February 1971:
Vol. 171. no. 3972, pp. 689 - 691
DOI: 10.1126/science.171.3972.689
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Articles

Lesch-Nyhan Syndrome: Altered Kinetic Properties of Mutant Enzyme

John A. McDonald 1 and William N. Kelley 1

1 Departments of Medicine and Biochemistry, Duke University Medical Center, Durham, North Carolina

Hypoxanthine-guanine phosphoribosyltransferase is virtually inactive in erythrocytes from patients with the classical Lesch-Nyhan syndrome. In one such patient, activity of this enzyme ranged from 8 to 34 percent of normal in erythrocytes when assayed with a very high concentration of magnesium 5-phosphoribosyl-1-pyrophosphate. In addition, the mutant enzyme exhibited sigmoidal kinetics with this substrate as well as an increased Michaelis constant for both guanine and hypoxanthine. These findings provide the first evidence for genetic heterogeneity within the group of patients with the Lesch-Nyhan syndrome.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Hypoxanthine phosphoribosyltransferase: two-dimensional gels from normal and Lesch-Nyhan hemolyzates.
G. Ghangas and G Milman (1977)
Science 196, 1119-1120
   Abstract »    PDF »
Phosphoribosylpyrophosphate synthetase is elevated in fibroblasts from patients with the Lesch-Nyhan syndrome.
D. Martin Jr and B. Maler (1976)
Science 193, 408-411
   Abstract »    PDF »
Monoamine oxidase activity decreased in cells lacking hypoxanthine phosphoribosyltransferase activity.
X. Breakefield, C. Castiglione, and S. Edelstein (1976)
Science 192, 1018-1020
   Abstract »    PDF »


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