Myosin isozyme distribution in rodent hindlimb skeletal muscle.

The purpose of this study was to examine the distribution of myosin isozymes in rodent (Rattus norvegicus) hindlimb skeletal muscles and regions of muscle known to have contrasting fiber-type composition. Muscle samples were analyzed for Ca2+-regulated myofibril adenosine triphosphatase (ATPase) activity, Ca2+-activated myosin ATPase activity, myosin isozyme profile, and myosin light chain profile. Four isozymes of myosin were identified based on native protein and light chain electrophoresis patterns: one associated primarily with slow-twitch muscle (SM) and three associated primarily with fast-twitch muscle (FM). Multiple linear regression analysis of Ca2+-regulated myofibril ATPase activity (pCA 4) vs. measured isozyme profile was used to estimate the myofibril ATPase activities of the individual isozymes (FM1 = 0.86, FM2 = 0.52, FM3 = 0.31, and SM = 0.15 mumol Pi formed . mg myofibril protein-1 . min-1 at 25 degrees C, n = 180, P less than 0.001). Differences in the native isozyme profiles and myofibril ATPase activities between muscles and muscle regions of similar fiber type composition indicate that a given fiber type may not necessarily express a single isozyme profile. These data are consistent with the hypothesis that, among rodent hindlimb skeletal muscles and inherently their motor units, a range of myosin isozyme profiles exists that may provide a broad range of mechanical expression.