Identiy of brain alcohol dehydrogenase with liver alcohol dehydrogenase

Alcohol Dehydrogenase with

Complexation of alcohol dehydrogenase (ADH) and trypsin with poly(diallyldimethyl-ammonium chloride) (PDADMAC) in dilute electrolyte solution was studied by turbidimetric titration, quasi-elastic light scattering (QELS), and electrophoretic light scattering (ELS). Both QELS and turbidimetric titration show that PDADMAC forms complexes with ADH and trypsin in 0.01M NaCl solution at pH ¢ 6.8 and ...

The physiological role of liver alcohol dehydrogenase.

1. Yeast alcohol dehydrogenase was used to determine ethanol in the portal and hepatic veins and in the contents of the alimentary canal of rats given a diet free from ethanol. Measurable amounts of a substance behaving like ethanol were found. Its rate of interaction with yeast alcohol dehydrogenase and its volatility indicate that the substance measured was in fact ethanol. 2. The mean alcoho...

Kinetic studies of liver alcohol dehydrogenase.

1. NADH2 prepared by enzymic reduction of pure NAD by the method of Rafter & Colowick (1957), and isolated as the sodium salt, gives higher maxrimum rates of reduction of acetaldehyde with liver alcohol dehydrogenase at pH 6 than a number of commercial preparations of high purity. Maximum values of 2-4 for the extinction ratio E260/E340 and 2% for the proportion of inactive material absorbing a...

Residual activity in carboxymethylated liver alcohol dehydrogenase.

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...