Initial Characterization of Aldehyde Dehydrogenase from Rat Testis Cytosol

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Abstract
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.degree. 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.mu.M for acetaldehyde to 4.mu.M for capronaldehyde and Ki decreases from about 4mM for butyraldehyde to 0.2mM for capronaldehyde.

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