Sodium plus potassium-activated, ouabain-inhibited adenosine triphosphatase from a fraction of rat skeletal muscle, and lack of insulin effect on it.

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.