Characterization of the biochemical basis of a complete deficiency of the adenine phosphoribosyl transferase (APRT)

Hum Genet. 1981;57(4):404-10. doi: 10.1007/BF00281694.

Abstract

In order to study the biochemical basis of a complete deficiency of adenine phosphoribosyl transferase (APRT) the enzyme was purified to homogeneity, its properties were characterized, and antibodies raised. The enzyme is indirectly involved in adenine uptake. Apparently, by forming AMP the internal concentration of adenine is kept low allowing it diffusion. The same APRT is present in various tissues as was revealed by antibody inactivations employing anti-erythrocyte APRT as well as by direct enzyme assays in cells from the APRT deficient patient. In vitro cultured fibroblasts derived from this patient had less than 0.02% enzyme activity. No cross-reacting material was found in erythrocytes obtained from an APRT deficient child.

MeSH terms

  • Adenine
  • Adenine Phosphoribosyltransferase / deficiency*
  • Adenine Phosphoribosyltransferase / immunology
  • Adenine Phosphoribosyltransferase / metabolism*
  • Antigen-Antibody Reactions
  • Cross Reactions
  • Erythrocytes / immunology
  • Female
  • Humans
  • Male
  • Pedigree
  • Pentosyltransferases / deficiency*
  • Pentosyltransferases / metabolism*
  • Tissue Distribution

Substances

  • Pentosyltransferases
  • Adenine Phosphoribosyltransferase
  • Adenine