Open AccessPurification and Characterization of Aldehyde Dehydrogenase from Bovine Liver
Author(s) -
LEICHT Wolfgang,
HEINZ Fritz,
FREIMÜLLER Barbara
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12083.x
Subject(s) - sedimentation equilibrium , chemistry , aldehyde dehydrogenase , sodium dodecyl sulfate , nad+ kinase , chromatography , acetaldehyde , biochemistry , enzyme , cysteine , michaelis–menten kinetics , ultracentrifuge , electrophoresis , gel electrophoresis , glyceraldehyde , dehydrogenase , enzyme assay , ethanol
Aldehyde dehydrogenase from bovine liver has been purified to homogeneity. Amino acid composition showed a high content of cysteine of 32 mol/mol enzyme. The enzyme is composed of four identical subunits as judged by sodium dodecyl sulfate gel electrophoresis and end‐group analysis. The molecular weight was determined to be 220 000 ± 10 000 by sedimentation equilibrium analysis in an analytical ultracentrifuge. The Michaelis constants for NAD + , glyceraldehyde and acetaldehyde were found to be 47 μM, 170 μM and 130 μM, respectively.