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Kinase activity and protein phosphorylation in control and malignant hyperthermic skeletal muscle
M Joffe1, N Savage, C du Sautoy
1Department of Medical Biochemistry, University of the Witwatersrand Medical School, Parktown, South Africa.
The International Journal of Biochemistry
|January 1, 1991
Abstract:
1. Native 6% Laemmli gels were used to resolve 7 protein kinase activity bands in control and malignant hyperthermia (MH)-susceptible porcine and human skeletal muscle extracts. 2. MH-susceptible samples were consistently more active than the controls. 3. Following halothane treatment, a 43 kDa component displayed increased phosphorylation by a calcium-calmodulin dependent kinase in MH-susceptible vs control human samples. 4. Increased phosphorylation of additional endogenous protein components of molecular mass 116 and 60 kDa was observed.