Related Experiment Video
Updated: Jan 25, 2026

Dosage-Adjusted Resistance Training in Mice with a Reduced Risk of Muscle Damage
Published on: August 31, 2022
[Changes in aldolase and creatine kinase activity during thermal muscle damage]
Abstract:
A study was made of changes in outflux, extractability and enzyme (aldolase and creatine kinase) activity of muscle proteins induced by thermal action in skeletal muscles of R. temporaria L. Under a 15-minutes action of temperatures under 36 degrees C, which do not produce any contracture or fall of excitability, changes in a fraction of protein outfluxed from muscles were observed. The thermal action accompanied by the fall and irreversible loss of excitability (above 36 degrees) resulted in the fall of extractability and enzyme activity of water-soluble proteins extracted from homogenized muscles in addition to prolonged changes in the fraction of outfluxed proteins. The increased binding of aldolase by actomyosin under thermal injury of muscle is established. Changes of outflux extractability and enzyme activity of proteins during the thermal alteration of muscle are considered with regard to data about the complexing of muscle proteins.
Related Concept Videos
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases
Cycloaddition Reactions: MO Requirements for Thermal Activation
Thermal expansion and Thermal stress: Problem Solving
To solve the problem, first, identify the known and unknown quantities. The initial length (L) of the bridge is 1275 m, the coefficient of linear expansion (α) for steel is 12 x 10-6/°C, and the change in temperature (ΔT) is 55...
Activation Energy
Receptor Tyrosine Kinases

