The heat denaturation process of myosin and the effect of the modification of amino groups of myosin with ti-naphthoquinone-4-sulfonic acid (NQS) on heat denaturation reaction were studied by using SDS polyacrylamide gel electrophoresis.Heavy chain and one of the light chains, g2, disappeared in the supernatant after centrifugation of heat treated myosin during two hours' heating, whereas two sorts of the light chains, gl and gs, were still found in the supernatant. In addition, a new peptide fraction appeared during heating.Heat denaturation of myosin was significantly suppressed by the modification of amino groups of myosin with NQS, where only heavy chain's electrophoretic pattern was influenced by NQS-modification.

Several workers have documented that rabbit "ghost" fibers and myofibrils irrigated with myosin can contract upon addition of Mg2+-ATP.1•`5) Tawada et al.5) have indicated that in the myosin-irrigated fibers thick filaments are reformed in lengths from one Z-mem brane to the other Z-membrane of a sarcomere, running

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