Key result
Target inactivation analysis of the ryanodine receptor from skeletal muscle sarcoplasmic reticulum revealed a target molecular weight of 138,000 +/- 21,000.
Effect estimate: 138,000 +/- 21,000
Target inactivation analysis reveals the target molecular weight of the skeletal muscle ryanodine receptor is 138,000 +/- 21,000, smaller than its binding polypeptide.
Target inactivation sizes RyR; extends early SR channel localization to molecular scale.
Target inactivation analysis was carried out on the ryanodine receptor. This receptor recently has been implicated as the channel involved in the calcium release process in excitation-contraction coupling and was localized to the junctional terminal cisternae of sarcoplasmic reticulum from skeletal muscle [Fleischer, S., Ogunbunmi, E. M., Dixon, M. C., & Fleer, E.A.M. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 7256-7259]. Irradiation of the junctional terminal cisternae resulted in an exponential decrease in ryanodine binding with radiation dose, thereby consistent with target theory. The target molecular weight was found to be 138,000 +/- 21,000, i.e., smaller than the polypeptide that binds ryanodine. The calcium pump protein in the same membrane preparation served as an internal control to validate the methodology.
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McGrew et al. (1987) studied this question. Target inactivation analysis (irradiation) vs. Calcium pump protein (internal control) was evaluated on Target molecular weight of the ryanodine receptor (138,000 +/- 21,000). Target inactivation analysis of the ryanodine receptor from skeletal muscle sarcoplasmic reticulum revealed a target molecular weight of 138,000 +/- 21,000.
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