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[含羞草三磷酸腺苷酶]

[Mimosa pudica adenosine triphosphatase].

作者信息

Liubimova-Engel'gardt M N, Burnasheva S A, Faĭn F S, Mitina N A, Poprykina Ia M

出版信息

Biokhimiia. 1978;43(4):748-60.

PMID:148923
Abstract

The morphological structure (pulvinus P1, P2 and P3) directly involved in the seismonastic movements of the Mimosa pudica leaf have been used to isolate: 1) "soluble" ATPase, loosely bound to pulvinus structures; 2) Ca, Mg-dependent ATPase, which is tightly bound to pulvinus structures and is extracted by a saline solution of high ionic strength, used to isolate actomyosin from muscles and non-muscle motile cells; 3) ATPase bound to the pulvinus membrane structures, which is solubilized by the detergents, e. g. Triton X-100 and Tween-80, and is similar to membrane ATPase. Physico-chemical and kinetic studies of the APSases have shown that Ca,Mg-ATPase is similar to the ATPases from muscle and non-muscle motile cells in a number of characteristics, e. g. solubility in saline solution of high ionic strength, aggregability in a solution of lower ionic strength, activation by bivalent metal ions, pH-optimum, specificity for substrates, etc. The protein composition of the ATPases has been determined by gel-electrophoresis in polyacrylamide gel. The molecular weight of purified Ca,Mg-ATPase from Mimosa pudica pulvinus is found to be 139 000. The role of ATPases in seismonastic movements of the Mimosa pudica leaf is discussed.

摘要

含羞草叶片感震运动直接涉及的形态结构(叶枕P1、P2和P3)已被用于分离:1)“可溶性”ATP酶,松散结合于叶枕结构;2)钙、镁依赖性ATP酶,紧密结合于叶枕结构,可被高离子强度盐溶液提取,该溶液用于从肌肉和非肌肉运动细胞中分离肌动球蛋白;3)结合于叶枕膜结构的ATP酶,可被去污剂(如Triton X - 100和吐温80)溶解,与膜ATP酶相似。对这些ATP酶的物理化学和动力学研究表明,钙、镁 - ATP酶在许多特性上与来自肌肉和非肌肉运动细胞的ATP酶相似,例如在高离子强度盐溶液中的溶解度、在较低离子强度溶液中的聚集性、二价金属离子的激活作用、最适pH值、对底物的特异性等。通过聚丙烯酰胺凝胶电泳测定了ATP酶的蛋白质组成。从含羞草叶枕中纯化的钙、镁 - ATP酶的分子量为139000。文中讨论了ATP酶在含羞草叶片感震运动中的作用。

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