TY - JOUR
T1 - The inhibitory effect of ethanol on retinol oxidation by human liver and cattle retina
AU - Mezey, Esteban
AU - Holt, Peter R.
N1 - Funding Information:
The authors thank Mrs. Lola Schoenfeld and Mrs. Susan Swiderski for excellent technical assistance. This study was supported in part by NIMH Grant RO 2 MH 14251 and NIH Grants AM 13436 and AM 05499.
PY - 1971/10
Y1 - 1971/10
N2 - The in vitro oxidation of ethanol and retinol by human liver and cattle retina was studied. Purification of human liver alcohol dehydrogenase yielded similar increases in the specific activity and recovery of ethanol and retinol oxidizing activities, and antibodies to the purified enzyme produced similar inhibition of the oxidation of both substrates. The specific activity of oxidation of ethanol as substrate was 150 times higher than of retinol by liver alcohol dehydrogenase, while the Michaelis-Menten constant was 50-fold smaller for retinol oxidation. In cattle retina, the specific activities and Michaelis-Menten constants for both ethanol and retinol oxidation were of comparable magnitude. Ethanol was found to be an inhibitor of retinol oxidation by both human liver and cattle retina. The inhibition was competitive with respect to retinol at ethanol concentrations of 1.8 × 10-4 M and below, and mixed or noncompetitive at higher ethanol concentrations. The inhibition constant, Ki, was 3.6 × 10-4 M for human liver alcohol dehydrogenase. The maximum inhibition of retinol oxidation by cattle retina that could be obtained by increasing ethanol concentrations was 38%. It is suggested that both ethanol and retinol are oxidized by the same enzyme in the liver, but not in the retina.
AB - The in vitro oxidation of ethanol and retinol by human liver and cattle retina was studied. Purification of human liver alcohol dehydrogenase yielded similar increases in the specific activity and recovery of ethanol and retinol oxidizing activities, and antibodies to the purified enzyme produced similar inhibition of the oxidation of both substrates. The specific activity of oxidation of ethanol as substrate was 150 times higher than of retinol by liver alcohol dehydrogenase, while the Michaelis-Menten constant was 50-fold smaller for retinol oxidation. In cattle retina, the specific activities and Michaelis-Menten constants for both ethanol and retinol oxidation were of comparable magnitude. Ethanol was found to be an inhibitor of retinol oxidation by both human liver and cattle retina. The inhibition was competitive with respect to retinol at ethanol concentrations of 1.8 × 10-4 M and below, and mixed or noncompetitive at higher ethanol concentrations. The inhibition constant, Ki, was 3.6 × 10-4 M for human liver alcohol dehydrogenase. The maximum inhibition of retinol oxidation by cattle retina that could be obtained by increasing ethanol concentrations was 38%. It is suggested that both ethanol and retinol are oxidized by the same enzyme in the liver, but not in the retina.
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U2 - 10.1016/0014-4800(71)90095-5
DO - 10.1016/0014-4800(71)90095-5
M3 - Article
C2 - 4398759
AN - SCOPUS:0015145188
SN - 0014-4800
VL - 15
SP - 148
EP - 156
JO - Experimental and Molecular Pathology
JF - Experimental and Molecular Pathology
IS - 2
ER -