Human Genetics

, Volume 88, Issue 6, pp 695–696

The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction

  • Therese Lightfoot
  • Rahul Joshi
  • George Nuki
  • Floyd F. Snyder
Short Communications

DOI: 10.1007/BF02265300

Cite this article as:
Lightfoot, T., Joshi, R., Nuki, G. et al. Hum Genet (1992) 88: 695. doi:10.1007/BF02265300

Summary

The change in DNA responsible for partial hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency in three brothers has been determined by polymerase chain amplification and sequencing. An A-to-G substitution at base 155 in exon 3 predicts a change in aspartic acid 52 to glycine. Allele-specific polymerase chain amplification verified the presence of the mutation in genomic DNA and provides a means of direct diagnostic assay.

Copyright information

© Springer-Verlag 1992

Authors and Affiliations

  • Therese Lightfoot
    • 1
  • Rahul Joshi
    • 1
  • George Nuki
    • 2
  • Floyd F. Snyder
    • 1
  1. 1.Department of Paediatrics and Department of Medical BiochemistryUniversity of CalgaryCalgaryCanada
  2. 2.Rheumatic Disease Unit, Department of MedicineUniversity of Edinburgh, Northern General HospitalEdinburghUK

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