[How many persons do we need for clinical trials? Analysis of the 2 x 2 table].
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Biomedical subjects
Publications and source records attributed to S E Vollset.
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The intracellular localization studies of human blood platelets by sucrose gradient and differential centrifugation, showed that palmitoyl-CoA hydrolase was mainly localized in the cytosol fraction. However, a localization also in the mitochondrial fraction seems possible as disruption of platelets by the French press and nitrogen decompression techniques resulted in mitochondrial damage. In human liver the palmitoyl-CoA hydrolase was localized in the mitochondrial and microsomal fractions. Palmitoyl-CoA synthetase was localized in the mitochondrial and microsomal fractions in both platelets and liver. The possible physiological implications of these differences, and the finding of a very high ratio of palmitoyl-CoA hydrolase/palmitoyl-CoA synthetase in platelets compared with liver, are discussed.
The assay conditions for palmitoyl-CoA synthetase (P-CoA S) and carnitine palmitoyltransferase (CPT) in homogenates of human blood platelets have been studied. The assay based on trapping of palmitoyl-CoA by carnitine in the presence of exogenous CPT gave higher activity of P-CoA S than the assay based on direct isolation of the palmitoyl-CoA formed. The activity of CPT was higher on exogenous palmitoyl-CoA than on endogenous palmitoyl-CoA formed from palmitic acid and CoA in the presence of endogenous P-CoA S. The activity of CPT was strongly dependent on the incubation time and the amount of platelets used. The initial activity of this enzyme in human blood platelets was higher than previously assumed.