Pea chloroplast carnitine acetyltransferase
نویسندگان
چکیده
منابع مشابه
Carnitine acetyltransferase in nervous tissue.
Some of the kinetic properties of carnitine acetyltransferase in brain homogenates have been reported with the use of a new, sensitive radiometric method for the determination of acetylcarnitine. Those properties and the distribution pattern of carnitine acetyltransferase in various rat tissues, subcellular fractions, and discrete areas of the brain have been compared with those obtained for ch...
متن کاملCytochemical localization of transferase activities: carnitine acetyltransferase.
Two methods for the cytochemical detection of free CoA and their utilization in the finestructural localization of carnitine acetyltransferase in rat heart are described. The first utilizes the reducing property of the SH group of CoA to reduce potassium ferricyanide to potassium ferrocyanide, which in the presence of uranyl ions forms an electron-dense precipitate of uranyl ferrocyanide. The s...
متن کاملThe substrate specificity of carnitine acetyltransferase.
1. A study of the acyl group specificity of the carnitine acetyltransferase reaction [acyl-(-)carnitine+CoASH right harpoon over left harpoon (-)-carnitine+acyl-CoA] has been made with the enzyme from pigeon breast muscle. Acyl groups containing up to 10 carbon atoms are transferred and detailed kinetic investigations with a range of acyl-CoA and acylcarnitine substrates are reported. 2. Acyl-C...
متن کاملProperties of partially purified carnitine acetyltransferase.
Subsequent reports from our laboratory showed that both carnitine (/3-hydroxy-y-trimethylammonium butyrate) and acetylcarnitinei increased oxygen uptake and oxidation of long chain fatty acids by heart homogenates incubated under conditions optimal for fatty acid oxidation (2, 3). Acetylcarnitine action could not be attributed simply to formation of carnitine via hydrolysis because acetylcarnit...
متن کاملPea chloroplast glutathione reductase: purification and characterization.
Glutathione reductase (EC 1.6.4.2) was purified from intact pea (Pisum sativum) chloroplasts by a method which includes affinity chromatography on ADP-agarose. Fractions from the affinity column which had glutathione reductase activity consisted of polypeptides of 60 and 32 kilodaltons. Separation of the proteins by electrophoresis on native gels showed that glutathione reductase activity was a...
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ژورنال
عنوان ژورنال: Proceedings of the Royal Society of London. Series B: Biological Sciences
سال: 2000
ISSN: 0962-8452,1471-2954
DOI: 10.1098/rspb.2000.0958