Interaction of enzymes with mixed micelles of phospholipid and detergent: Analysis of the phospholipase A2-dipalmitoyl phosphatidylcholine-triton X 100 system
✍ Scribed by Dennis, Edward A.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1974
- Tongue
- English
- Weight
- 715 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0091-7419
No coin nor oath required. For personal study only.
✦ Synopsis
Physical studies on the formation and structure of mixed micelles of the nonionic surfactant Triton X-100 and phospholipids and enzymatic studies on the action of phospholipase A, toward these mixed micelles are presented. Results of nmr intensity, line width, and T I determinations, as well as gel chromatography and centrifugation experiments on the interaction of Triton X-100 with egg and dipalmitoyl phosphatidylcholine, are presented and discussed. The structure of mixed micelles is discussed in terms of a working schematic model which is consistent with the experimental results. Kinetic studies on phospholipase A, (Naja naja) action are then analyzed in terms of this model. The temperature dependence of phospholipase A, action toward dipalmitoyl phosphatidylcholine is considered in terms of the effect of thermotropic phase transitions on mixed micelle formation. The phospholipase A, -dipalmitoyl phosphatidylcholine-Triton X-I00 system is then considered as an artificial model system for studying the effect of lipid phase separations on biological activity.