Vara F, Serrano R
Biochem J. 1981 Sep 1;197(3):637-43. doi: 10.1042/bj1970637.
Microsomal membranes from Cicer arietinum (chick-pea) roots contained an ATP phosphohydrolase activity that could be solubilized by high-ionic-strength media. The enzyme has been purified to homogeneity by affinity and ion-exchange chromatography. It has the properties of an ATP diphosphohydrolase (apyrase, EC 3.6.1.5) that hydrolyses different nucleoside di- and tri-phosphates but has no activity towards monophosphoric esters and pyrophosphate. No stimulation by K+ could be demonstrated for either the membrane-bound or the purified enzyme, and therefore it would seem not to be related to the K+ -dependent ATPase postulated to mediate K+ transport in plants.
鹰嘴豆根的微粒体膜含有一种ATP磷酸水解酶活性,该活性可被高离子强度介质溶解。通过亲和色谱和离子交换色谱已将该酶纯化至同质。它具有ATP二磷酸水解酶(焦磷酸酶,EC 3.6.1.5)的特性,可水解不同的核苷二磷酸和三磷酸,但对单磷酸酯和焦磷酸无活性。无论是膜结合酶还是纯化酶,均未显示出K+的刺激作用,因此它似乎与推测介导植物中K+转运的K+依赖性ATP酶无关。