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Plant Physiology 67:261-265 (1981) © 1981 American Society of Plant Biologists Phospholipid Metabolism in Plant MitochondriaII. SUBMITOCHONDRIAL SITES OF SYNTHESIS OF PHOSPHATIDYLCHOLINE AND PHOSPHATIDYLETHANOLAMINE 1Department of Botany, University of Wyoming, Laramie, Wyoming 82071
CDPcholine:1,2-diacylglycerol cholinephosphotransferase (EC 2.7.8.2) and CDPethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase (EC 2.7.8.1) were detected in mitochondrial fractions from castor bean (Ricinus communis) endosperm. These activities were not due to contamination of the fractions with endoplasmic reticulum. The enzymes were localized on both the inner and outer mitochondrial membranes. Only minor kinetic differences between the phosphatidylcholine-synthesizing activities of intact mitochondria and of the endoplasmic reticulum were found. The Km of the mitochondrial enzyme for CDP-choline was about 2 units less than that for the enzyme of the endoplasmic reticulum (8.0 and 10.0 micromolar, respectively). The mitochondrial enzyme activity was maximal above 10 millimolar Mg2+, whereas maximum endoplasmic reticulum activity was achieved by 4 millimolar. The endoplasmic reticulum enzyme was more stable at 37 C than was that of the mitochondria. The mitochondrial cholinephosphotransferase represented about 1 to 2% of the total activity isolated from castor bean endosperm.
1 This research was supported by National Science Foundation Grant PCM78-06817. This article has been cited by other articles:
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