Human liver aldehyde dehydrogenases: new method of purification of the major mitochondrial and cytosolic enzymes and re-evaluation of their kinetic properties
LG Rashkovetsky, W Maret, AA Klyosov - Biochimica et Biophysica Acta …, 1994 - Elsevier
A new purification procedure, based on dye-adsorption and affinity chromatography, has
been developed for the isolation of the two major ALDH isozymes from human liver: ALDH-1
(cytosolic, pI 5.2) and ALDH-2 (mitochondrial, pI 4.9). The procedure affords milligram
quantities of ALDH-1 and-2 at 850-and 275-fold purifications, respectively, from 50 g of liver
in two days. Kinetic parameters for acetaldehyde oxidation were determined with these
purified enzymes, because there is a wide discrepancy in the absolute magnitude of these …
been developed for the isolation of the two major ALDH isozymes from human liver: ALDH-1
(cytosolic, pI 5.2) and ALDH-2 (mitochondrial, pI 4.9). The procedure affords milligram
quantities of ALDH-1 and-2 at 850-and 275-fold purifications, respectively, from 50 g of liver
in two days. Kinetic parameters for acetaldehyde oxidation were determined with these
purified enzymes, because there is a wide discrepancy in the absolute magnitude of these …