Chemical Cross-linking of Actin and Myosin Subfragment-1 in Rigor Complex

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Chemical cross-linking of actin and myosin subfragment-1 (S-1) was investigated under various conditions. Action and S-1 were cross-linked with the aid of zero-angstrom cross-linker 1-ethl-3-(3-(dimethylamino)propyl) carbodiimide(EDC). Three new bands having larger molecular weight than those of two subunits of S-1and one new, band having larger molecular weight than the sub-units of S-1 appeared on electorophoretograms after the cross-linking reaction. These new bands were formed by cross-linking between action and subcomponents of S-1. The extent of cross-linking decreased with increasing the ionic strength reaction mixtures and also decreased with increasing the concentration of ATP. The extent of cross-linking between S-1 and action prepared from fresh muscle in rigor (stored at 0℃ for 24h) and even that of those proteins prepared from muscle stored for more prolonged period (168h). The elucidate the effect of paratropomyosin on action-S-1 interaction, the extent of actin-S-1 complex formation in the absence or presence of paratropomyosin during the cross-linking reaction was investigated. As a result, the formation of new bandswas reduced after the addition of paratropomyosin, while almost no change of intensity of S-1 heavy chain (90kDa) was observed. The result indicates that paratropomyosin is involved in the weakening of action-myosin interaction during the deveropment of the resolution of rigor.
九州大学の論文