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  • Title: [Aldehyde-dehydrogenase from human liver: Purification, partial characterization and influence of malondialdehyde].
    Author: Wache H, Böhme I, Sorger H, Nilius R.
    Journal: Biomed Biochim Acta; 1990; 49(10):979-89. PubMed ID: 2080909.
    Abstract:
    A procedure to separate the isozymes E1 and E2 of aldehyde dehydrogenase (ALDH, aldehyde: NAD oxidoreductase, EC 1.2.1.3) from human liver, avoiding 5'-AMP-Sepharose, was worked out. It results in fairly purified isozymes. The isoelectric points could be re-estimated for E1 at pH 5.21 +/- 0.04 and for E2 at pH 4.90 +/- 0.05. The pH-optimum of both the isozymes is dependent on the buffer used, the best buffer being sodium pyrophosphate/HCI. In this buffer the enzyme activity is also dependent on ionic strength. Malondialdehyde (MDA), at concentrations which are found in patient serum, is converted by the ALDH. The Km-values of this reaction are 1.71 mmol/l for MDA and 0.19 mmol/l for NAD (E1) and 0.21 mmol/l for MDA and 0.24 mmol/l for NAD (E2) resp. The highest rates of conversion are reached at concentrations of 0.08 mmol/l MDA (E1) and 0.16 mmol/l MDA (E2). At higher concentrations of MDA substrate excess inhibition is observed (Kss = 0.17 mmol/l for E1 and 0.20 mmol/l for E2).
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