gamma-Hydroxybutyrate has been found to be widely distributed in both neural and extraneural tissues in the rat. The kidney and brown fat have more than 10 times higher concentrations of gamma-hydroxybutyrate than does the brain. This observation suggests that gamma-hydroxybutyrate may participate in the metabolism of many organs, and that GABA may not be the precursor in extraneural tissues.
A method for obtaining electrophoretically homogeneous rat liver alcohol dehydrogenase (EC 1.1.1.1) at a specific activity of 2-2.5 μmol/min per mg of protein is presented. Anti-sera prepared against the purified enzyme inhibit alcohol dehydrogenase by up to 75% and cause precipitation of virtually all the enzyme. The antisera were shown by immunoelectrophoresis of a partially purified liver homogenate to be specifically directed against alcohol dehydrogenase and were used to demonstrate that the alcohol dehydrogenases of rat brain and liver share common antigens. The total activity of alcohol dehydrogenase in rat brain homogenates is normally quite low, with as much as 10% of the total activity attributable to the activity in the blood contained within the brain; in cases of severe liver damage (induced experimentally with carbon tetrachloride) this contribution may rise to as much as 60%.
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