The polymerization of protein through disulfide bonding during the heating of carp myosin

The polymer of protein through SS bonding on the top of 5% SDS-PAGE gel was found to be made up of only a myosin heavy chain from the analysis of two-step SDS-PAGE, and from the results it was a dimer, trimer, tetramer, and above-decamer with 1.8% SDS-PAGE gel. The polymerization was suppressed in the presence of N-ethylmaleimide, dithiothreitol, or EDTA. The polymerization of myosin light chains as well as myosin heavy chain was promoted in the presence of transition ion (Cu+, Cu2+), while Ca2+ and Mg2+ did not affect the polymerization. From the above results, it was made clear that the polymerization of protein through SS bonding during the heating of myosin is the reaction that the SH groups of myosin heavy chain are oxidized in the presence of catalysts such as copper ion, and contribute to the smooth and swift formation of the polymer larger than decamer.