Literature DB >> 1252480

[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)].

M Levy, M Joncourt, J Thiessard.   

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.

Entities:  

Mesh:

Substances:

Year:  1976        PMID: 1252480     DOI: 10.1016/0005-2760(76)90049-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  Purification of apo-3-D-(-) hydroxybutyrate dehydrogenase from rat liver mitochondria.

Authors:  J C Vidal; E A Guglielmucci; A O Stoppani
Journal:  Mol Cell Biochem       Date:  1977-07-05       Impact factor: 3.396

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.