Rat liver mitochondrial ADP-ribose pyrophosphatase in the matrix space with low Km for free ADP-ribose

Biochem J. 1994 May 1;299 ( Pt 3)(Pt 3):679-82. doi: 10.1042/bj2990679.

Abstract

A study involving markers of subcellular and submitochondrial fractions, gradient centrifugation, latency measurements and extraction with digitonin, demonstrates the association of a specific ADP-ribose pyrophosphatase with rat liver mitochondria and its localization in the matrix space. The enzyme hydrolyses ADP-ribose to AMP, with a Km of 2-3 microM. The results support the occurrence of a specific turnover pathway for free ADP-ribose and its relevance in mitochondria.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / isolation & purification
  • Adenosine Diphosphate Ribose / metabolism*
  • Animals
  • Chromatography, Gel
  • Extracellular Matrix / enzymology*
  • Mitochondria, Liver / enzymology*
  • Pyrophosphatases / isolation & purification
  • Pyrophosphatases / metabolism*
  • Rats

Substances

  • Adenosine Diphosphate Ribose
  • ADP-ribose pyrophosphatase I
  • Pyrophosphatases