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Purification and Characterization of Beef and Pig Liver Aldehyde Dehydrogenases
Author(s) -
Guan Kurt Liang,
Pak Youngmi Kim,
Tu Guang Chou,
Cao Qing,
Weiner Henry
Publication year - 1988
Publication title -
alcoholism: clinical and experimental research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.267
H-Index - 153
eISSN - 1530-0277
pISSN - 0145-6008
DOI - 10.1111/j.1530-0277.1988.tb00270.x
Subject(s) - aldehyde dehydrogenase , enzyme , biochemistry , aldh2 , acetaldehyde , disulfiram , cytosol , mitochondrion , chemistry , serine , aconitase , biology , microbiology and biotechnology , ethanol
Beef liver cytosolic, mitochondrial, and pig liver mitochondrial aldehyde dehydrogenases (ALDH) had been purified to homogeneity. The two mitochondrial enzymes as with other mammalian mitochondrial enzymes had properties very similar to that of the corresponding human enzyme. These include immunological as well as basic kinetic properties such as low K m for aldehyde, activation by Mg 2+ ions, and lack of inhibition by disulfiram. A major difference between these two enzymes and the human mitochondrial enzyme was that they contained an N‐terminal‐blocked amino acid. Cytosolic ALDHs from human and horse liver have been shown to possess an N‐acetyl serine as the N‐terminal residue; beef cytosolic ALDH was also found to be blocked. Tissue preparations and subcellular fractions from beef or pig liver could be used to study acetaldehyde oxidation. This is the subject of the accompanying paper (Cao Q‐N, Tu G‐C, Weiner H, Alcohol Clin Exp Res 12xxx‐xxx, 1988).