[Beta-Hydroxybutyrate dehydrogenase of rat liver inner mitochondrial membrane. Its isolation, characterization, and reactivation by lecithins differing in their apolar regions. The influence of the addition of cholesterol on its level of reactivation (author's transl)]

Abstract

The beta-hydroxybutyrate dehydrogenase has been isolated and purified from the inner mitochondrial membrane of the rat liver. It consists in a dimer of molecular weight 77 000 composed by two subunits of molecular weight 38 000 each. The level of its reactivation by lecithin is influenced by the length and degree of unsaturated of their aliphatic chains. The addition of cholesterol inhibits the reactivation.