Abstract
Pyrenedodecanoyl-CoA was beta-oxidized by isolated rat liver peroxisomes at a rate which was about 50% of that observed with palmitoyl-CoA. Measurement of the quantity of NADH formed from a limiting amount of pyrenedodecanoyl-CoA suggested that it was subjected to two to three cycles of beta-oxidation. Pyrenedodecanoyl-CoA was a very poor substrate for carnitine palmitoyltransferase, exhibiting less than 1% of the rate obtained with palmitoyl-CoA; it also was a strong inhibitor of this enzyme. With rat liver microsomal alpha-glycerophosphate acyltransferase the rate of reaction with pyrenedodecanoyl-CoA was only 3-4% of that observed with palmitoyl-CoA.
Original language | English |
---|---|
Pages (from-to) | 130-133 |
Number of pages | 4 |
Journal | Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids |
Volume | 958 |
Issue number | 1 |
DOIs | |
State | Published - 19 Jan 1988 |
Externally published | Yes |
Keywords
- Beta oxidation
- Peroxisomal beta oxidation
- Pyrene dodeconoic acid
- Pyrene fatty acid