Characterization of serine palmitoyltransferase activity in Chinese hamster ovary cells.

@article{Merrill1983CharacterizationOS,
  title={Characterization of serine palmitoyltransferase activity in Chinese hamster ovary cells.},
  author={Alfred H. Merrill},
  journal={Biochimica et biophysica acta},
  year={1983},
  volume={754 3},
  pages={284-91}
}
Serine palmitoyltransferase (palmitoyl-CoA: L-serine C-palmitoyltransferase (decarboxylating) EC 2.3.1.50) catalyzes the first unique and regulatory reaction of sphingolipid biosynthesis. Its activity was demonstrated in Chinese hamster ovary cells (CHO-K1) by measuring the incorporation of radiolabel from L-[3H]serine into 3-ketosphinganine, which was found to be the predominant chloroform-soluble product under optimal assay conditions. Most of the total activity (14.8 +/- 4.2 pmol/min per 10… CONTINUE READING