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Purine metabolism in cultured human fibroblasts derived from patients deficient in hypoxanthine phosphoribosyltransferase, purine nucleoside phosphorylase, or adenosine deaminase.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Thompson, Linda F. Willis, Randall C. Stoop, J. W. Seegmiller, J. Edwin |
| Copyright Year | 1978 |
| Abstract | Rates of purine synthesis de novo, as measured by the incorporation of [14C]formate into newly synthesized purines, have been determined in cultured human fibroblasts derived from normal individuals and from patients deficient in adenosine deaminase, purine nucleoside phosphorylase, or hypoxanthine phosphoribosyltransferase, three consecutive enzymes of the purine salvage pathway. All four types of cell lines are capable of incorporating [14C]formate into purines at approximately the same rate when the assays are conducted in purine-free medium. The purine overproduction that is characteristic of a deficiency in either the transferase or the phosphorylase and that results from a block in purine reutilization can be demonstrated by the resistance of [14C]formate incorporation into purines to inhibition by hypoxanthine in the case of hypoxanthine phosphoribosyltransferase-deficient fibroblasts and by resistance to inhibition by inosine in the case of purine nucleoside phosphorylase-deficient fibroblasts. |
| File Format | PDF HTM / HTML |
| DOI | 10.1073/pnas.75.8.3722 |
| PubMed reference number | 99741 |
| Journal | Medline |
| Volume Number | 75 |
| Issue Number | 8 |
| Alternate Webpage(s) | http://www.pnas.org/content/75/8/3722.full.pdf |
| Alternate Webpage(s) | https://doi.org/10.1073/pnas.75.8.3722 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |