Cao Q N, Tu G C, Weiner H
Department of Biochemistry, Purdue University, West Lafayette, IN 47907.
Biochem Pharmacol. 1989 Jan 1;38(1):77-83. doi: 10.1016/0006-2952(89)90152-4.
A colony of Wistar-strain rats bred at Purdue University was composed of animals with two different isozyme patterns of liver cytosolic aldehyde dehydrogenase (EC 1.2.1.3, ALDH) as determined by isoelectric focusing. One cytosolic isozyme pattern had a major activity band with a pI = 5.8 and a minor activity band at pI = 6.2. The other pattern contained three major isozymes with pI values of 5.3, 5.4 and 5.6 along with the pI 6.2 isozyme and a trace of the 5.8 one. The 5.8 and 6.2 isozymes were recognized by antibodies produced against horse and beef liver cytosolic ALDH, whereas the set of three (5.3-5.6) were not. The cytosolic isozymes were inhibited by low levels of disulfiram and had Km values for acetaldehyde in the 100 microM range, properties typical for cytosolic ALDHs. All animals contained the same isozymes of liver mitochondrial ALDH. These were a major activity with a pI = 5.2 and minor activities associated with isozymes of pI = 6.4 and 6.6. These isozymes were recognized by antibodies produced against pure horse and beef liver mitochondrial ALDHs. Both cytosolic and mitochondrial ALDHs were found in fetal liver as early as day 15 of gestation. The total activity for mitochondrial ALDH increased between day 15 and day 21 whereas that for cytosolic ALDHs remained relatively constant during development. It appeared that both cytosolic and mitochondrial ALDH were present by at least the third trimester and could afford the fetus some protection against the toxic action of endogenous or exogenous aldehydes.
