2,8-Dihydroxyadenine lithiasis in a Japanese patient heterozygous at the adenine phosphoribosyltransferase locus.

Abstract

All reported cases of 2,8-dihydroxyadenine (DHA) lithiasis have been due to functional homozygous deficiency of adenine phosphoribosyltransferase (APRT). Here we describe the first case of DHA lithiasis in a patient who has functional APRT activity in cultured lymphoblasts. The patient is heterozygous for Japanese-type (type II) APRT deficiency as demonstrated by starch-gel electrophoresis and DNA sequence analysis. We also demonstrate the use of starch-gel electrophoresis for differentiation between the type II mutant enzyme and the wild-type enzyme.

• Authors: A Sahota, J Chen, M A Behzadian, R Ravindra, H Takeuchi, P J Stambrook, J A Tischfield
• Journal: American journal of human genetics (Am J Hum Genet) Vol. 48 Issue 5 Pg. 983-9 (May 1991) ISSN: 0002-9297 [Print] United States
• PMID: 1673292 (Publication Type: Case Reports, Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Nucleotides
• 2,8-dihydroxyadenine
• Adenine Phosphoribosyltransferase
• Adenine

Topics

• Adenine (analogs & derivatives, metabolism)
• Adenine Phosphoribosyltransferase (genetics, metabolism)
• Adult
• Genetic Carrier Screening
• Heterozygote
• Humans
• Japan
• Kidney Calculi (chemistry)
• Lymphocytes (enzymology)
• Male
• Mutation (genetics)
• Nucleotides (metabolism)
• Polymorphism, Restriction Fragment Length