Myosin filament depolymerizes in a low ionic strength solution containing L-histidine.
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.
Hayakawa
T
T
Meat Science Laboratory, Graduate School of Agriculture, Hokkaido University, N-9, W-9, Kita-ku, Sapporo, Hokkaido 060-8589, Japan. t-haya@anim.agr.hokudai.ac.jp
Ito
T
T
Wakamatsu
J
J
Nishimura
T
T
Hattori
A
A
D000818:Animals; D002645:Chickens; D006639:Histidine / Q000737:chemistry*; D015879:Myosin Subfragments / Q000737:chemistry; D009218:Myosins / Q000737:chemistry*; D009994:Osmolar Concentration; D012996:Solutions
D015879:Myosin Subfragments; D012996:Solutions; D006639:Histidine; D009218:Myosins