منابع مشابه
The interaction of triiodothyroacetic acid with horse liver alcohol dehydrogenase.
Triiodothyroacetic acid is a competitive inhibitor of horse liver alcohol dehydrogenase with respect to the coenzyme. The Ki value for triiodothyroacetic acid in this system is 1.3 to 1.9 AuM. Triiodothyroacetic acid appears to interact with a hydrophobic portion of the protein since it is able to displace the hydrophobic compound, 8-anilino1 -naphthalene sulfonic acid from liver alcohol dehydr...
متن کاملInhibition 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 کاملpH-dependent Conformational States of Horse Liver Alcohol Dehydrogenase*
The quenching of liver alcohol dehydrogenase protein fluorescence at alkaline pH indicates two conformational states of the enzyme with a pK,, of 9.8 -t0.2, shifted to 10.6 f 0.2 in I&O. NAD’ and 2-p-toluidinonaphthalene-6-sulfonate, a fluorescent probe competitive with coenzyme, bind to the acid conformation of the enzyme. The pK,, of the proteinfluorescence quenching curve is shifted toward 7...
متن کاملZinc in Horse Liver Alcohol Dehydrogenase* by Bert L. Vallee
The alcohol dehydrogenase (ADH’) of yeast has twice the molecular weight of the ADH of horse liver (l), contains 4 gm. atoms of zinc (2), and binds 4 moles of DPN per mole of protein (1). The liver ADH binds 2 moles of coenzyme per mole (3). These facts prompted the prediction that the liver ADH should contain 2 gm. atoms of zinc per mole of protein (2). The presence of 2 atoms of zinc in liver...
متن کاملHorse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis
During catalysis by liver alcohol dehydrogenase (ADH), a water bound to the catalytic zinc is replaced by the oxygen of the substrates. The mechanism might involve a pentacoordinated zinc or a double-displacement reaction with participation by a nearby glutamate residue, as suggested by studies of human ADH3, yeast ADH1, and some other tetrameric ADHs. Zinc coordination and participation of wat...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43953-7