Effects of Phospholipids in the Action of Acetyl-CoA Carboxylase from Rat Liver
Open Access
- 1 February 1977
- journal article
- research article
- Published by Walter de Gruyter GmbH in Zeitschrift für Naturforschung C
- Vol. 32 (1-2) , 97-100
- https://doi.org/10.1515/znc-1977-1-216
Abstract
Acetyl-CoA carboxylase (E.C. 6.4.1.2) was isolated from rat liver. The purified enzyme contains phospholipids with a rather large amount of phosphatidylinositol (26%). Incubation of the purified acetyl-CoA carboxylase with phospholipase A2 (E.C. 3.1.1.4) or with phospholipase D (E.C. 3.1.1.4) diminishes the phospholipid content by 70%, this treatment leading to a complete inactivation of the enzyme. After removal of the phospholipases, the lipid-depleted enzyme can be reactivated to a certain degree by incubation with a phospholipid extract from rat liver, with phosphatidylinositol alone, or with serum albumin.This publication has 3 references indexed in Scilit:
- Role of phospholipid in the activation of Na+, Ka+-activated adenosine triphosphatase of beef brainArchives of Biochemistry and Biophysics, 1965
- Phospholipid requirement of Na+, K+-activated adenosine triphosphatase from rat brainArchives of Biochemistry and Biophysics, 1964
- A SIMPLE METHOD FOR THE ISOLATION AND PURIFICATION OF TOTAL LIPIDES FROM ANIMAL TISSUESJournal of Biological Chemistry, 1957