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- W2064748020 abstract "1. Long-chain fatty acyl-CoA synthetase (acid:CoA ligase (AMP), EC 6.2.1.3; trivial name: palmityl-CoA synthetase) has been studied in rat-liver homogenate and cellular subfractions with the aid of a new assay procedure for the enzyme. The principles of the method are as follows: Rat-liver homogenate or subfractions are incubated with palmitate, CoA, ATP and dl-[Me-3H] carnitine in Tris buffer (ph 7.5). The palmityl-CoA formed is quantitatively transformed to palmityl-dl-[Me-3H] carnitine by excess amounts of carnitine palmityltransferase. The palmityl-dl-[Me-3H] carnitine is extracted from the incubation mixture by n-butanol. The radioactivity in the butanol phase is proportional to the palmityl-CoA synthetase activity. 2. Addition of particle-free supernatant of the cytoplasmic extract to the incubation mixture has a stimulatory effect on the palmityl-CoA synthetase activity in isolated mitochondria and microsomes. The stimulatory factor in the supernatant is likely to be a protein or a factor bound to protein. 3. Differential centrifugation of rat-liver homogenate shows that the palmityl-CoA synthetase has a bimodal intracellular localization. Approximately 70% of total activity is localized in the microsomes, and approximately 30% in the mitochondria. The total activity is about 1.4 units per g wet wt. of liver. 4. Sucrose density-gradient centrifugation confirms the bimodal intracellular localization revealed by differential centrifugation. 5. The enzyme is relatively firmly bound to membranes both in mitochondria and microsomes." @default.
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- W2064748020 date "1967-03-01" @default.
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- W2064748020 title "Long-chain acyl-CoA synthetase in rat liver. A new assay procedure for the enzyme, and studies on its intracellular localization" @default.
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- W2064748020 doi "https://doi.org/10.1016/0005-2744(67)90167-2" @default.
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