Purification and properties of a membrane-bound aldehyde dehydrogenase from rat liver microsomes

Abstract

A membrane-bound aldehyde dehydrogenase was solubilized from rat liver microsomes and purified about 150-fold by chromatography on ω-aminohexyl- and 5′-AMP-Sepharose columns with a recovery of about 40%. The purified enzyme was homogeneous upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis and its monomeric molecular weight was estimated to be 51,000. In aqueous solution, it existed as large, polymeric aggregates. Its activity towards straight-chain aliphatic aldehydes increased as their carbon chain length was increased at least up to dodecanal, whereas aldehyde dehydrogenase in the cytosolic fraction of rat liver was most active with hexanal as substrate.