Initial characterization of aldehyde dehydrogenase from rat testis cytosol

Biol Chem Hoppe Seyler. 1990 Jan;371(1):95-101. doi: 10.1515/bchm3.1990.371.1.95.


Aldehyde dehydrogenase was purified 187-fold from cytosol of rat testis by chromatographic methods and gel filtration with a yield of about 50%. The enzyme exhibits absolute requirement for exogenous sulfhydryl compounds and strong dependence on temperature. Addition of 0.4mM Ca2 or Mg2 ions results in 50% inhibition. Optimally active at pH 8.5 and 50 degrees C, aldehyde dehydrogenase displays broad substrate specificity; saturation curves with acetaldehyde and propionaldehyde are non-hyperbolic, with Hill coefficients comprised between 0.8 and 0.7. Strong substrate inhibition can be observed with both aromatic and long-chain alyphatic aldehydes. According to mathematical models, Km decreases from 246 microM for acetaldehyde to 4 microM for capronaldehyde and Ki decreases from about 4mM for butyraldehyde to 0.2 mM for capronaldehyde.

MeSH terms

  • Aldehyde Dehydrogenase / antagonists & inhibitors
  • Aldehyde Dehydrogenase / isolation & purification*
  • Aldehyde Dehydrogenase / metabolism
  • Animals
  • Calcium / pharmacology
  • Cytosol / enzymology
  • Hydrogen-Ion Concentration
  • Kinetics
  • Magnesium / pharmacology
  • Male
  • Rats
  • Rats, Inbred Strains
  • Temperature
  • Testis / enzymology*


  • Aldehyde Dehydrogenase
  • Magnesium
  • Calcium