Brain microsomes catalyze the arylation of lysophosphatidylcholine (IysoPtdCho) in the presence and absence of added CoA derivatives. The catalytic activity is distributed widely in various subcellular fractions from rat or bovine cerebral cortex as measured by the conversion of l-['4C]palmitoyl-sn-
Acylation of lysophosphatidylcholine in nervous tissue
โ Scribed by F. J. Doherty; C. E. Rowe
- Book ID
- 111170642
- Publisher
- John Wiley and Sons
- Year
- 1979
- Tongue
- English
- Weight
- 261 KB
- Volume
- 33
- Category
- Article
- ISSN
- 0022-3042
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Phospholipases A 1 and A 2 frequently coexist in biological systems. Generation of lysophosphatidylcholine (LPC) in such systems cannot be assigned to any of these types of enzymes unless the position of the fatty acid in the lysocompound can be unambiguously determined. We here present a simple met
1-Ac yl-2-[ 9, 10-3H]oleoyl-~-glycero-3-phosphorylcholine was prepared by acylating l-acyl-~-glycero-3-phosphorylcholine with labelled oleic acid, in the presence of dicyclohexylcarbodiimide (DCC), as condensing agent. A simple column chromatographic procedure allowed both purification of the labell