アクトミオシンから単離されたF-アクチンの長さ
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概要
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Recently Barany and Jaisle (1960) reported a simple method to isolate F-actin from natural actomyosin in good yield by a use of polyethylene sulphonate (PES). This has made it possible to study the molecular dimension of the separated F-actin, which may originate from the thin filaments of myofibrils. It is of interest to compare its particle length with that of usual F-actin (Straub F-actin), which forms a network structure in solution (Kasai et al., 1960). Flow birefringence technique was used. As seen in Fig. 1, the extinction angle (therefore, also its rotary diffusion constant) of F-actin from myosin B at low velocity gradients was much larger than that of F-actin from reconstituted actomyosin or of Straub F-actin. It is to be noted that PES depolymerizes F-actin to some extent, as shown in Fig. 1 and Table 1. Nevertheless the difference between the F-actins from natural and reconstituted actomyosins is clear cut: the former is much shorter in particle length than the latter, as summarized in Table 5. The particle length of F-actin from natural actomyosin ranged from 0.9 to 2.6μ (Tables 3 and 5), which is very close to the distribution of particle length of natural actomyosin (1-3 and 0.8-2.7μ, without and with ATP, respectively)(cf. Noda and Maruyama, 1958). In Table 5, the results of a series of determinations with varied F-actin preparations are summarized: F-actin from the reconstituted actomyosin showed a particle length about twice as long as that of F-actin from natural actomyosin. More remarkable is that F-actin from myosin B did not show any sign of network formation, such as decrease of extinction angle when repeatedly determined at low velocity gradients or semipermanent birefringence after removal of shear stress. It is of some interest to mention that the particle length became significantly longer, when F-actin from myosin B was depolymerized by dialysis against ATP and thereafter was repolymerized by the addition of KCl and MgCl_2. Yet, it is certainly shorter than the corresponding Straub F-actin, treated in the same way (Table 5). Our previous work also suggested that the particle length of F-actin isolated from natural actomyosin without use of PES is of a similar magnitude to that of natural actomyosin (Noda and Maruyama, 1960). F-actin directly isolated from myofibrils without use of acetone ("natural F-actin") also had a particle length of similar dimension. What makes the difference between usual Straub F-actin and F-actin prepared without use of acetone? This is presumably not due to the direct action of the acetone on the actin molecule and the probable answer will be the subject of a forthcoming article (Maruyama, 1964b). This work was supported by a grant-in-aid from the Muscular Dystrophy Associations of America.
- 社団法人日本動物学会の論文
- 1963-09-15
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