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- W2012128602 abstract "(1) dl-[3-14C]Methylmalonyl-Coenzyme A was enzymatically synthesized from propionyl-CoA and [14C]NaHCO3 (specific activity 5 μCi/μmole) employing propionyl-CoA carboxylase activity prepared from bovine liver. A net yield of 25%, based on propionyl-CoA of the purified product was achieved, having a specific activity of 4.1 μCi/μmole. (2) Purity of the dl-[14C]methylmalonyl-CoA was found to be about 90% and was based on (a) extent of decarboxylation under “back reaction conditions” of propionyl-CoA carboxylase, (b) thin layer chromatography of the thioester, (c) gas-liquid chromatography of the dimethylester derivative of [3-14C]methylmalonic acid, following deacylation. (3) The purified product was fairly stable when stored at −80°C in vacuo, undergoing decarboxylation at a rate of 4% per month. (4) Methylmalonyl-CoA mutase activity was measured in human liver preparations employing purified dl-[3-14C]methylmalonyl-CoA. Activity was based on the rate of formation of [14C]succinyl-CoA, the latter determined as the free acid isolated on thin layer chromatography. Activity was linear over a 20-minute time course in the presence of 1.25 units of enzyme and also with respect to enzyme concentration over a 1–11 unit range of enzyme activity under routine assay conditions." @default.
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- W2012128602 date "1973-04-01" @default.
- W2012128602 modified "2023-09-25" @default.
- W2012128602 title "A direct radioassay of methylmalonyl-coenzyme A mutase using enzymatically synthesized dl-[3-14C]methylmalonyl-CoA" @default.
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- W2012128602 doi "https://doi.org/10.1016/0003-2697(73)90057-2" @default.
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