Abstract
A 3-fold increase in aldehyde dehydrogenase (A1DH) was found in the cytosolic fraction of mouse liver homogenates during pregnancy. The increase in A1DH activity began at day 10 of pregnancy, peaked at parturition, and declined in a biphasic manner with half-lives of 4.15 and 47.7 days. Enzymes from control (ß A1DH), pregnant (it A1DH)and phenobarbital-treated (cp A1DH) were partially purified and compared. All had molecular weights of approximately 60,000 daltons. Substrate specificities were similar except that <p A1DH had a lower Km for propionaldéhyde than ß or jt and both it and cp oxidized 4-carboxybenzaldehyde poorly compared to ß. Electrophoretic and thermal dénaturation studies showed some similarities between ß and it, but <p A1DH behaved quite differently. It was concluded that pregnancy caused an increase in one of the AlDHs already present in control mice, while phénobarbital treatment resulted in induction of a unique cytosolic A1DH.