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Myosin is solubilized in a neutral and low ionic strength solution containing l-histidine

Author:
Hayakawa, T., Ito, T., Wakamatsu, J., Nishimura, T., Hattori, A.
Source:
Meat science 2009 v.82 no.2 pp. 151-154
ISSN:
0309-1740
Subject:
muscle protein, meat protein, sarcomeres, myosin, ionic strength, solubilization, histidine, dialysis, potassium chloride, transmission electron microscopy, pH, solutions
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.
Agid:
751528