| Autor: |
Ken Jyh Fang Liaw, Ryuichi Tatsumi, Yoshihide Ikeuchi, Sunao Mori, Sumie Hashimoto, Minoru Yamanoue, Tatsumi Ito, Miyako Sugimitsu, Toshiya Hayashi |
| Rok vydání: |
2004 |
| Předmět: |
|
| Zdroj: |
Journal of the Faculty of Agriculture, Kyushu University. 49:111-118 |
| ISSN: |
0023-6152 |
| Popis: |
Chemical cross-linking of actin and myosin subfragment-1 (S-1) was investigated under various conditions. Actin and S-1 were cross-linked wlth the aid of zero-angstrom cross-linker 1-ethyl-3-(3-(dimethylamino)propyl) carbodiimide (EDC). Three new bands having larger molecular weight than those of two subunits of S-1 and one new, band having smaller molecular weight than the sub-units of S-1 appeared on electrophoretograms after the cross-linking reaction. These new bands were formed by cross-1inking between actin and subcomponents of S-1. The extent of cross-linking decreased with increasing the ionic strength of reaction mixtures and also decreased with increasing the concentration of ATP. The extent of cross-linking between S-1 and actin prepared from fresh muscle was not appreciably smaller than that of those proteins prepared from postmortem muscle in rigor (stored at O 'C for 24 hr) and even that of those proteins prepared from muscle stored for more prolonged period (168 hr). To elucidate the effect of paratropomyosin on actin-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 bands was reduced after the addition of paratropomyosin, while almost no change of the intensity of S-1 heavy chain (90kDa) was observed. The result indicates that paratropoTnyosin is involved in the weakening of actin-myosin interaction during the development of the resolution of rigor. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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