Purification and characterization of mouse hypoxanthine-guanine phosphoribosyltransferase

J Biol Chem. 1975 Jan 10;250(1):120-6.

Abstract

Hypoxanthine-guanine phosphoribosyltransferase (HGPR transferase) (EC 2.4.2.8) has been purified approximately 4500-fold to apparent homogeneity from mouse liver. The procedure involves the use of affinity chromatography and was designed to be readily adaptable to small scale isolations. The enzyme appears to be composed of 3 subunits of identical molecular weight (27,000 per subunit). The subunit molecular weight has also been determined by the analysis of radioactively labeled HGPR transferase immunoprecipitated from wild type and mutant (HGPR transferase) mouse tissue culture cell lines.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Buffers
  • Cell Line
  • Centrifugation, Density Gradient
  • Chromatography, Affinity
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Electrophoresis, Polyacrylamide Gel
  • Guanine Nucleotides
  • Humans
  • Hydrogen-Ion Concentration
  • Hypoxanthines
  • Inosine Nucleotides
  • Isotope Labeling
  • L Cells / enzymology
  • Liver / enzymology*
  • Macromolecular Substances
  • Mice
  • Molecular Weight
  • Pentosyltransferases / immunology
  • Pentosyltransferases / isolation & purification*
  • Pentosyltransferases / metabolism
  • Radioimmunoassay
  • Sulfur Radioisotopes
  • Tritium
  • Ultrafiltration

Substances

  • Buffers
  • Guanine Nucleotides
  • Hypoxanthines
  • Inosine Nucleotides
  • Macromolecular Substances
  • Sulfur Radioisotopes
  • Tritium
  • Pentosyltransferases