Purification and characterization of a long-chain acyl-CoA hydrolase from rat liver microsomes.

@article{Berge1979PurificationAC,
  title={Purification and characterization of a long-chain acyl-CoA hydrolase from rat liver microsomes.},
  author={Rolf Kristian Berge},
  journal={Biochimica et biophysica acta},
  year={1979},
  volume={574 2},
  pages={321-33}
}
A long-chain acyl-CoA hydrolase from rat liver microsomes has been purified by solvent extraction and gel chromatography to homogeneity as judged by polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate. The enzyme was a monomer of molecular weight 59 000. In a sucrose gradient it sedimented at 4.3 S. The isoelectric point, pI was 6.9, and the Stokes radius was approx. 31 A. The enzyme hydrolyzed long-chain fatty acyl-CoA (C7--C18) with maximum activity for… CONTINUE READING
8 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

Similar Papers

Loading similar papers…