Rogus E, Price T, Zierler K L
J Gen Physiol. 1969 Aug;54(2):188-202. doi: 10.1085/jgp.54.2.188.
An ATPase, activated by Na(+) plus K(+) in the presence of Mg(++) and inhibited by ouabain, has been obtained from rat skeletal muscle. Unlike ATPase's with similar properties obtained from other preparations, this ATPase was found only in the fraction containing fragmented sarcoplasmic reticulum. It is suggested that in rat skeletal muscle this ATPase may reside in sarcoplasmic reticulum and not in sarcolemma. This ATPase differed in its pH optimum and in its cation sensitivity from that of rat brain and from that of human muscle reported by Samaha and Gergely (1965, 1966). Because insulin accelerates Na(+) efflux from muscle, efforts were made to determine whether or not this effect of insulin could be attributed to increased Na(+) + K(+)-activated ATPase activity. Insulin, administered either in vivo or in vitro, had no demonstrable effect on the enzyme system, nor did it protect against inhibition by ouabain.
在大鼠骨骼肌中已获得一种ATP酶，该酶在Mg(++)存在的情况下被Na(+)加K(+)激活，并被哇巴因抑制。与从其他制剂中获得的具有类似性质的ATP酶不同，这种ATP酶仅存在于含有破碎肌浆网的组分中。有人提出，在大鼠骨骼肌中，这种ATP酶可能存在于肌浆网而非肌膜中。这种ATP酶在最适pH值和阳离子敏感性方面与大鼠脑的ATP酶以及Samaha和Gergely（1965年、1966年）报道的人类肌肉的ATP酶有所不同。由于胰岛素可加速肌肉中Na(+)的外流，因此人们努力确定胰岛素的这种作用是否可归因于Na(+) + K(+)激活的ATP酶活性的增加。无论是在体内还是体外给予胰岛素，对该酶系统均无明显影响，也不能防止其被哇巴因抑制。
