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  • Journal
    Digital Access ACPOnline v. 1-5, 1998-2002.
  • Article
    Blaner WS, Churchich J.
    J Biol Chem. 1979 Mar 25;254(6):1794-8.
    The enzyme succinic semialdehyde dehydrogenase from pig brain has been 2000-fold purified by a combination of DEAE-cellulose, hydroxyapatite, and AMP-Sepharose chromatography. This preparation has a molecular weight of 160,000 and a specific activity of 5.3 mumol/min.mg at 25 degrees C. The inhibition of succinic semialdehyde dehydrogenase by carbonyl compounds, i.e. P-pyridoxal and o-phthalaldehyde was investigated in detail. The enzyme is reversible, inhibited by preincubation with P-pyridoxal (mixing molar ratio, 300:1) at either 25 degrees or 37 degrees C. Reduction with NaBH1 results in the incorporation of approximately 4 mol of P-pyridoxyl residues/mol of enzyme. NAD+ protects the enzyme against inactivation by P-pyridoxal, whereas the substrate succinic semialdehyde failed to prevent the reaction of P-pyridoxal with lysine residues of the protein. The binding of approximately 10 mol of o-phthalaldehyde/mol of enzyme results in irreversible loss of catalytic activity. The reaction is fast and easily monitored by absorption and fluorescence spectroscopy.
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