Pyrimidine 5′-nucleotidase activity in normal and deficient human lymphoblastoid cells
✍ Scribed by D. A. Hopkinson; D. M. Swallow; A. Marinaki; E. H. Harley
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 588 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0141-8955
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A new case of a defect in red cell pyrimidine 5'-nucleotide (P5N) activity was found in a large family from Guadeloupe in the West Indies. The propositus presented a characteristic hemolytic anemia with red cell basophilic stippling, an increased GSH level, and a shift of the peak in absorbance of n
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 monophosph
## Abstract We used a shuttle vector based on the Epstein‐Barr virus origin of plasmid replication (oriP) to determine the types of mutations induced by depurination in human cells. Plasmid DNA was incubated at pH 2 at 40°C for various times to induce up to 20 apurinic (AP) sites per 9.7‐kb plasmid