Hydrolysis of long-chain fatty acyl-CoA in homogenates of human blood platelets: the existence of a platelet palmitoyl-CoA hydrolase.
Scand J Clin Lab Invest, 1978/12;38(8):699-706.
PMID: 33445
Impact factor: 2.209
Abstract
The existence of a very active long-chain fatty acyl-CoA hydrolase in homogenates of human blood platelets is reported. The highest activity was found with palmitoyl-CoA as the substrate. Palmitoyl-CoA hydrolase activity was not found in intact platelets indicating that the enzyme is localized within the platelet membrane. No palmitoyl-CoA hydrolase activity was found in fasting plasma. Mg2+, Mn2+, Ca2+ and Triton X-100 inhibited the palmitoyl-CoA hydrolase activity. Sulphydryl reagents had no effect, whereas high concentrations of D- and L-carnitine inhibited the activity. Carnitine palmitoyltransferase did not interfere with the assay of palmitoyl-CoA hydrolysis as the activity of carnitine-palmitoyl hydrolase was less than 1% of the palmitoyl-CoA hydrolase activity.
MeSH terms
Acyl Coenzyme A; Blood Platelets; Blood Proteins; Carnitine; Cell Membrane; Cholesterol Esters; Coenzyme A; Humans; Hydrolysis; Indicators and Reagents; Nucleotides; Palmitates; Palmitoyl-CoA Hydrolase; Phospholipids; Serum Albumin, Bovine; Sulfhydryl Compounds; Temperature; Thiolester Hydrolases; Triglycerides
More resources
EndNote: Download