Ionic Strength - Explore the Science & Experts | ideXlab

Scan Science and Technology

Contact Leading Edge Experts & Companies

Ionic Strength

The Experts below are selected from a list of 240 Experts worldwide ranked by ideXlab platform

Ionic Strength – Free Register to Access Experts & Abstracts

Akihito Hattori – One of the best experts on this subject based on the ideXlab platform.

Toru Hayakawa – One of the best experts on this subject based on the ideXlab platform.

  • Myosin filament depolymerizes in a low Ionic Strength solution containing l-histidine
    Meat science, 2009
    Co-Authors: Toru Hayakawa, Toshiaki Ito, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito Hattori
    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.

  • Myosin is solubilized in a neutral and low Ionic Strength solution containing L-histidine.
    Meat science, 2009
    Co-Authors: Toru Hayakawa, Toshiaki Ito, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito Hattori
    Abstract:

    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 1 mM KCl and 5 mM 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.

Takanori Nishimura – One of the best experts on this subject based on the ideXlab platform.

  • Myosin filament depolymerizes in a low Ionic Strength solution containing l-histidine
    Meat science, 2009
    Co-Authors: Toru Hayakawa, Toshiaki Ito, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito Hattori
    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.

  • Myosin is solubilized in a neutral and low Ionic Strength solution containing L-histidine.
    Meat science, 2009
    Co-Authors: Toru Hayakawa, Toshiaki Ito, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito Hattori
    Abstract:

    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 1 mM KCl and 5 mM 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.

Jun-ichi Wakamatsu – One of the best experts on this subject based on the ideXlab platform.

  • Myosin filament depolymerizes in a low Ionic Strength solution containing l-histidine
    Meat science, 2009
    Co-Authors: Toru Hayakawa, Toshiaki Ito, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito Hattori
    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.

  • Myosin is solubilized in a neutral and low Ionic Strength solution containing L-histidine.
    Meat science, 2009
    Co-Authors: Toru Hayakawa, Toshiaki Ito, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito Hattori
    Abstract:

    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 1 mM KCl and 5 mM 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.

Toshiaki Ito – One of the best experts on this subject based on the ideXlab platform.

  • Myosin filament depolymerizes in a low Ionic Strength solution containing l-histidine
    Meat science, 2009
    Co-Authors: Toru Hayakawa, Toshiaki Ito, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito Hattori
    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.

  • Myosin is solubilized in a neutral and low Ionic Strength solution containing L-histidine.
    Meat science, 2009
    Co-Authors: Toru Hayakawa, Toshiaki Ito, Jun-ichi Wakamatsu, Takanori Nishimura, Akihito Hattori
    Abstract:

    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 1 mM KCl and 5 mM 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.