Abstract
Bovine lens aldehyde dehydrogenase is located predominantly in the cortical and nuclear regions, although the specific activity is highest in the epithelial cells. A novel two-step procedure has been used to purify aldehyde dehydrogenase from bovine lens to homogeneity. A comparison using published assay methods for aldehyde dehydrogenases showed that the dimeric lens enzyme had the highest specific activity of any cytoplasmic aldehyde dehydrogenase, although the kcat value was not exceptional. Computer curve-fitting showed that the minimum degree of the rate equation with propionaldehyde and acetaldehyde as substrates was 2:2. The relationship (a2 X b1)/(a1 X b2) was used to show the marked effect of temperature, and to a lesser extent pH, on the non-linear steady-state kinetics. These results indicate that the rate-determining step at low aldehyde concentrations (probably aldehyde binding) is accelerated by increasing temperature to a much greater degree than the rate-determining step at high aldehyde concentration (probably NADH release).
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