Kinetic dependence of phospholipase A 2 activity on the detergent Triton X-100.
Kinetic dependence of phospholipase A 2 activity on the detergent Triton X-100.
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发表时间：
1973-03
影响因子：
6.5
通讯作者：
E. Dennis
中科院分区：
文献类型：
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作者：
E. Dennis
本文对眼镜蛇毒液中磷脂酶A(2)的一种形式与非离子去污剂Triton X-100存在时对卵磷脂酰胆碱和合成的二棕榈酰甘油磷酰胆碱的活性进行了动力学分析。为了连续监测酶的活性，使用了自动记录pH-STAT装置。根据Triton X-100胶束将磷脂双层转化为混合Triton X-100-磷脂胶束时磷脂物理状态的变化来解释本研究中获得的结果，这与该酶对胶束形式的底物的要求一致，而不是单体或双层。根据底物的胶束性质，描述和讨论了高浓度Triton X-100对磷脂酶A(2)活性的明显抑制。
A kinetic analysis is presented for the dependence of one form of phospholipase A(2) from cobra (Naja naja) venom on the presence of the nonionic detergent Triton X-100 for its activity towards egg phosphatidylcholine and synthetic dipalmitoyl glycerophosphorylcholine as substrates. An automatic recording pH-stat apparatus was employed in order to continuously monitor enzyme activity. The results obtained in this study are interpreted in terms of a change in the physical state of the phospholipid when Triton X-100 micelles convert phospholipid bilayers into mixed Triton X-100-phospholipid micelles; this is consistent with the requirement of this enzyme for substrates which are in micellar form rather than either monomers or bilayers. An apparent inhibition of phospholipase A(2) activity at high concentrations of Triton X-100 is described and discussed in terms of the micellar nature of the substrate.