Proteolytic activation of the plant plasma membrane H(+)-ATPase by removal of a terminal segment.
Proteolytic activation of the plant plasma membrane H(+)-ATPase by removal of a terminal segment.
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通过去除末端片段来蛋白水解激活植物质膜 H(+)-ATP 酶。
DOI：
10.1016/s0021-9258(18)77361-4
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
M. Sommarin
中科院分区：
文献类型：
--
作者：
M. Palmgren;C. Larsson;M. Sommarin
燕麦根质膜囊泡在ATP存在下与胰蛋白酶或胰凝乳蛋白酶孵育可增加ATP水解速率和质膜H（+）-ATPase依赖ATP的质子泵。质子泵被刺激超过200%，而ATP水解活性被刺激约30%。质子泵和ATP水解的Km（ATP）从约0.3 mM降低到0.1 mM以下。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳的胰蛋白酶处理的质膜显示在100 kDa的带和93 kDa的带的外观减少。用H（+）-ATP酶抗体进行的Western印迹分析表明，这两条带代表H（+）-ATP酶，并表明释放了一个7-kDa的片段。用羧肽酶A大量处理也激活了H（+）-ATP酶，表明7-kDa片段来自C末端。
Incubation of oat root plasma membrane vesicles in the presence of ATP with trypsin or chymotrypsin increased the rate of ATP hydrolysis and ATP-dependent proton pumping by the plasma membrane H(+)-ATPase. Proton pumping was stimulated more than 200%, whereas ATP hydrolytic activity was stimulated about 30%. The Km (ATP) for both proton pumping and ATP hydrolysis was lowered from about 0.3 mM to below 0.1 mM. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of trypsin-treated plasma membranes revealed a decrease in a 100-kDa band and the appearance of a 93-kDa band. Western blot analysis using antibodies against the H(+)-ATPase showed that both of these bands represented the H(+)-ATPase and suggested that a 7-kDa segment was released. Extensive treatment with carboxypeptidase A also activated the H(+)-ATPase indicating that the 7-kDa segment originated from the C terminus.