A model for the activation of porcine pancreatic phospholipase A2 for the hydrolysis of dipalmitoylphosphatidylcholine liposomes
โ Scribed by D. Lichtenberg; M. Menashe; R.L. Biltonen
- Publisher
- Elsevier Science
- Year
- 1985
- Weight
- 612 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0166-6622
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A structure-activity relationship is presented that satisfactorily predicts the rates of hydrolysis of a series of acetylglycine derivatives by porcine aminoacylase. It is apparent that the substrate specificity of aminoacylase is mainly kinetic in origin, the observed correlation with Taft's E s pa
Phospholipase A 2 (PLA 2 ) is an enzyme that cleaves fatty acids from the sn-2 position of membrane phospholipids. Intracellular PLA 2 has been shown to be important for the generation of arachidonic acid, which leads to the synthesis of a wide range of eicosanoid paracrine hormones. Furthermore, se