Reversible Inhibition of Sheep Liver Sorbitol Dehydrogenase by Thiol Compounds
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چکیده
منابع مشابه
Inhibition of Horse Liver Alcohol Dehydrogenase by Methyltin Compounds
The study of inorganic tin (SnCl(2), SnCl(4)) and methyltin compounds (MeSnCl(3), Me(2)SnCI(2), Me(3)SnCl) effects on the enzymatic activity of alcohol dehydrogenase (ADH) in the reaction of ethanol oxidation has been carried out. The experimental results of the study show that inorganic tin and methyltin substances induce slight inhibition of the catalytic activity of horse liver alcohol dehyd...
متن کاملSheep Liver 6-Phosphogluconate Dehydrogenase INHIBITION BY KUCLEOSIDE PHOSPHATES AND BY OTHER METABOLIC INTERMEDIATES*
A variety of metabolic intermediates of the glycolytic pathway and tricarboxylic acid cycle have been found to be inhibitors of 6-phosphogluconate dehydrogenase isolated from sheep liver. All nucleoside 5’-triphosphates and 5’diphosphates are inhibitors with Ki values averaging 0.8 mM, nucleoside 5’-monophosphates are also inhibitory with Ki values averaging 6 mu. The 2’and 3’monophosphates of ...
متن کاملSheep liver 6-phosphogluconate dehydrogenase. Inhibition by nucleoside phosphates and by other metabolic intermediates.
A variety of metabolic intermediates of the glycolytic pathway and tricarboxylic acid cycle have been found to be inhibitors of 6-phosphogluconate dehydrogenase isolated from sheep liver. All nucleoside 5’-triphosphates and 5’diphosphates are inhibitors with Ki values averaging 0.8 mM, nucleoside 5’-monophosphates are also inhibitory with Ki values averaging 6 mu. The 2’and 3’monophosphates of ...
متن کاملThe mechanism of inhibition of horse liver alcohol dehydrogenase by thyroxine and related compounds.
Thyroxine and related compounds have been found to be excellent inhibitors of horse liver alcohol dehydrogenase. The thyroid hormones appear to act by interfering with the normal coenzyme-binding mechanism. Triiodothyronine and thyroxine are uncompetitive inhibitors with regard to the coenzyme. In addition to inhibiting the enzyme activity, the thyroid hormone also quenches the enhanced fluores...
متن کاملReversible Oxidation of Cyclic Secondary Alcohols by Liver Alcohol Dehydrogenase
During a study of cyclic alcohol oxidation by a partially purified rat liver enzyme system (l), it was noted that ethanol was also oxidized by this preparation. Since the ratio of the rate of ethanol oxidation to the rate of cyclohexanol oxidation remained constant during purification, the possibility arose that the activity with cyclic substrates was due to the conventional alcohol dehydrogena...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1996
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1996.0142t.x