Characterization of ATPase in sarcoplasmic reticulum from two strains of dystrophic mice

Abstract

The ATPase activities and phosphoenzyme levels have been determined in sarcoplasmic reticulum (SR) membranes prepared from two animal models of muscular dystrophy, myodystrophic (myd/myd) and strain 129 dystrophic (129 dy/dy) mice. In both myd/myd and 129 dy/dy SR membranes, the basal ATPase activities are elevated above control levels, while the Ca-dependent ATPase activities are normal. The addition of 0.1% Triton X-100 not only lowers the basal ATPase activity of myodystrophic control SR membranes by 60%, but also lowers the elevated basal ATPase activity of myd/myd SR membranes to a similar level. The Ca-dependent ATPase activities of myodystrophic control and myd/myd SR membranes are increased approximately threefold by the addition of Triton. The addition of 0.1% Triton X-100 lowers the basal ATPase activities of 129 control and 129 dy/dy SR membranes to similar levels, but stimulates the CA-dependent ATPase activity of 129 dy/dy SR membranes to a level that is only 60% of that of 129 control SR membranes. The level of phosphoenzyme intermediate is decreased approximately 15% in myd/myd SR membranes and approximately 30% in 129 dy/dy SR membranes.