Cytoplasmic aldehyde dehydrogenase from bovine lens was purified to apparent homogeneity by using ion-exchange and affinity chromatography. Sedimentation-equilibrium ultracentrifugation, gel-filtration chromatography and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis show that the enzyme is a dimer of Mr 114000, with subunits of Mr 57000. The enzyme does not dissociate into monomers in the presence of Ca2+ or Mg2+. The enzyme has a pI of 5.0, an activation energy of 35.1kJ/mmol and a pK value of 8.6 with acetaldehyde as substrate. The enzyme is a prolate ellipsoid with a Stokes radius of 4nm. Progesterone, deoxycorticosterone and chlorpropamide inhibited enzyme activity, and this inhibition may play a role in cataract formation in patients maintained on systemic corticosteroids and in tablet-dependent diabetics.
Research Article| November 01 1983
Bovine lens aldehyde dehydrogenase. Purification and preliminary characterization
Biochem J (1983) 215 (2): 351–359.
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H H Ting, M J C Crabbe; Bovine lens aldehyde dehydrogenase. Purification and preliminary characterization. Biochem J 1 November 1983; 215 (2): 351–359. doi: https://doi.org/10.1042/bj2150351
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