Role of Myosin Heavy Chains from Rabbit Skeletal Muscle in the Heat-induced Gelation Mechanism

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概要

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• Some physico-chemical and heat-induced gelling properties of myosin heavy chains (MHCs) from rabbit skeletal muscle were studied. MHCs were found to be almost devoid of ATPase activity, possibly because of the absence of myosin light chains. MHCs formed precipitates below and ionic strength of 0.3, and above this ionic strength MHCs became soluble. On heating to 65°C at low concentrations of the protein, MHCs lost their solubility and formed aggregates even at high ionic conditions. Partially irreversible change in the conformation of MHC (from helical to random coil) also occurred in heated MHCs. The heat-induced gel strength of MHCs was found to be almost equal to that of intact myosin molecules with ide tical protein concentrations. This suggests that the gelling potential of myosin is solely confined in MHC. Although myosin light chains do not seem to contribute to the gelling power of myosin, possibly they provide some stability to the gel if the pH is varied above the optimum value, i.e., 6.0. The addition of actin to a MHC system weakened the gel strength of the latter proportionally to the quantity of added actin.

• 社団法人 日本農芸化学会の論文

著者

• Yasui Tsutomu

  Department Of Animal Science Faculty Of Agriculture Hokkaido Unviersity

• Samejima Kunihiko

  Department Of Food Science Rakuno Gakuen University

• Yamauchi Hiroshi

  Department Of Chemistry Faculty Of Science Kanazawa University

• ASGHAR Ali

  Department of Animal Science, Faculty of Agriculture, Hokkaido University

• YASUI Tsutomu

  Department of Animal Science, Faculty of Agriculture, Hokkaiso University

• SAMEJIMA Kunihiko

  Department of Dairy Science, The College of Dairying

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