PubAg

Main content area

Myosin filament depolymerizes in a low ionic strength solution containing l-histidine

Author:
Hayakawa, T., Ito, T., Wakamatsu, J., Nishimura, T., Hattori, A.
Source:
Meat science 2010 v.84 no.4 pp. 742-746
ISSN:
0309-1740
Subject:
meat, myosin, ionic strength, histidine, solubilization, dissociation, meat protein, amino acid composition, essential amino acids, muscle protein, transmission electron microscopy, potassium chloride
Abstract:
Myosin, one of the major myofibrillar proteins, forms a filamentous polymer and is insoluble in physiological and low ionic strength solutions. We have shown that myosin is soluble in a low ionic strength solution containing l-histidine. In this study, to clarify the role of l-histidine in the solubilization of myosin, we investigated effects of l-histidine on the filament formation and the morphology of myosin at a low ionic strength. In the presence of l-histidine, myosin formed a filamentous polymer in a physiological ionic strength solution and dispersed in a low ionic strength solution. Transmission electron microscopy showed that light meromyosin (LMM), the rod region of myosin, in a low ionic strength solution containing l-histidine was longer than that in a high ionic strength solution without l-histidine. l-histidine causes the elongation of LMM region of myosin contributing to the weakening of the myosin filament and the dissociation of myosin in a low ionic strength solution.
Agid:
778053