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Updated: Jun 13, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Myosin is solubilized in a neutral and low ionic strength solution containing l-histidine
T Hayakawa1, T Ito, J Wakamatsu
1Meat Science Laboratory, Graduate School of Agriculture, Hokkaido University, N-9, W-9, Kita-ku, Sapporo, Hokkaido 060-8589, Japan.
Abstract:
Myosin, one of the major myofibrillar proteins, is insoluble at low and physiological ionic strength and soluble at high ionic strength. In this study, the behavior and morphology of myosin solubilized in a low ionic strength solution containing l-histidine (l-His) was investigated. More than 80% of myosin was solubilized in a low ionic strength solution with dialysis against a solution containing 1mM KCl and 5mM l-His. Transmission electron microscopy with rotary shadowing demonstrated that the rod of myosin in a low ionic strength solution containing l-His is longer than that of myosin in a high ionic strength solution. The elongation of the myosin rod in a low ionic strength solution containing l-His would inhibit the formation of a filament, resulting in the solubilization of myosin.
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