Characterization of Coturnix quail liver alcohol dehydrogenase enzymes.
Livers from male or female Coturnix quail possess up to four electrophoretically distinct bands of alcohol dehydrogenase (ADH) activity. Three pyrazole-sensitive bands of enzymatic activity, designated ADH-1, ADH-2, and ADH-3, are cathodic at pH 8.2, and the fourth, ADH-An, is neutral to slightly anodic and insensitive to pyrazole. ADH-2 and ADH-3, and occasionally ADH-1, are present in livers from immature females. The predominant enzyme in immature male livers is ADH-3. At sexual maturity all three pyrazole-sensitive enzymes are present in livers from male birds, and livers from females possess predominantly ADH-3. ADH-2 and ADH-3, purified from female livers, are dimers of 80,000 daltons possessing 4 mol of Zn2+/mol of native protein. Both ADH-2 and ADH-3 were inhibited by 4-methylpyrazole with KI values of 430 and 335 nM, respectively. These values are similar to those of human class I isoenzymes. Neither enzyme oxidized methanol or ethylene glycol, which distinguished them from mammalian pyrazole-sensitive ADH isoenzymes. Both ADH-2 and ADH-3 showed specificity toward hydrophobic primary alcohols and were most active toward benzyl alcohol and n-octanol.
Nussrallah
B A
BA
Department of Biochemistry, University of Nebraska, Lincoln 68583-0718.
Dam
R
R
Wagner
F W
FW
D000426:Alcohol Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D003370:Coturnix; D005260:Female; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008297:Male; D008970:Molecular Weight; D013379:Substrate Specificity
D000596:Amino Acids; D007527:Isoenzymes; D046911:Macromolecular Substances; D000426:Alcohol Dehydrogenase