Laboratory of Chemistry and Technology of Animal Products,Division of Applied Biological Chemistry,Department of Bioscience and Biotechnology,Faculty of Agriculture,Kyushu University
Laboratory of Chemistry and Technology of Animal Products,Division of Applied Biological Chemistry,Department of Bioscience and Biotechnology,Faculty of Agriculture,Kyushu University
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.
Mendeley出力
