We developed a specific spectrophotometric assay for the quantitative determination of phospholipase D-catalyzed transphosphatidylation activity. The assay measures p-nitrophenol liberated by phospholipase D-catalyzed reaction of phosphatidyl-p-nitrophenol and ethanol in an aqueous-organic emulsion
The transphosphatidylation activity of phospholipase D
β Scribed by Chang-Hua Yu; Song-Yan Liu; Vincenzo Panagia
- Publisher
- Springer
- Year
- 1996
- Tongue
- English
- Weight
- 462 KB
- Volume
- 157
- Category
- Article
- ISSN
- 0300-8177
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β¦ Synopsis
Transphosphatidylation activity is a characteristic and remarkable property of phospholipase D (PLD) and has been studied in plants and mammalian tissues. This reaction is often used to confirm the properties and/or abnormalities of PLD activity. The mechanism for activating PLD transphosphatidylation seems multiple. Although significant changes of transphosphatidylation activity have been found in some pathological animal models, the biological significance of PLD transphosphatidylation remains largely unknown.
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## Abstract Two approaches on enzymatic phospholipid modification were studied: (1) transphosphatidylation of the 1,2βdilauroylβ__sn__βglyceroβ3βphosphocholine (DLPC) and ethanolamine in biphasic and anhydrous organic solvent systems by phospholipase D (PLD) and (2) incorporation of oleic acid into
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