MEASUREMENT AND SUBCELLULAR-DISTRIBUTION OF CHOLOYL-COA SYNTHETASE AND BILE ACID-COA=AMINO ACID N-ACYLTRANSFERASE ACTIVITIES IN RAT-LIVER
- 1 January 1978
- journal article
- research article
- Vol. 19 (1), 24-31
Abstract
An improved method for assaying choloyl-CoA synthetase activity (EC 6.2.1.7) and 2 methods for specific measurement of bile acid-CoA:amino acid N-acyltransferase activity (EC 2.3.1) are described. The methods are shown to be reproducible, linear with respect to time and enzyme protein and result in estimates of enzymic activity that conform to the theoretical stoichiometry of the individual reactions. Utilizing these methods, the subcellular distribution of the rat liver enzymic activity catalyzing the formation of glycine and taurine conjugates of bile acids is shown. Choloyl-CoA synthetase is associated with the microsomal membranes and bile acid-CoA:amino acid N-acyltransferase activity with the postmicrosomal supernatant. No significant amino acid N-acyltransferase activity is present in the lysosome fraction. These studies provide methods that will permit further study of the individual enzymic reactions involved in the intrahepatic conjungation of bile acids with amino acids.This publication has 3 references indexed in Scilit:
- Characterization of liver cholic acid coenzyme A ligase activity. Evidence that separate microsomal enzymes are responsible for cholic acid and fatty acid activation.Journal of Biological Chemistry, 1977
- Coenzyme A derivatives of bile acids—chemical synthesis, purification, and utilization in enzymic preparation of taurine conjugatesJournal of Lipid Research, 1976
- Removal of Fatty Acids from Serum Albumin by Charcoal TreatmentJournal of Biological Chemistry, 1967