Studies on Muscle Proteins III. Behaviours of Actins in 7M Urea-Containing Buffer Solution
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The preparations of G- and F-actin from beef, pork and chicken were performed by themethods of Straub and Krans et al. and they were analyzed through DEAE cellulose columnchromatography and starch gel electrophoresis in 7M urea containing buffer solution (pH 8.6) by the method almost the same as those described in the previous paper.From the results obtained out of chromatography, it was evident that the principal peak of F-actin (not G-actin) corresponded to that of the maximal peak of the chromatogram of the meat-urea solution in all kinds of the animal tested, as was noted in the previous study.And from the results of starch gel electrophoresis, the conspicuous two bands, situated in the middle of each run, which had been found in the patterns of raw and cooked meat-urea solutions, were found in F-actin, at the position identical with the one mentioned above.Besides, the fraction corresponded to the principal peak on the DEAE cellulose columnchromatogram was collected and condensed, and the component in it was analyzed bySGE technique. The result showed the perfect coincidence of the both components, that is, one was the component that appeared on the chromatogram as a principal peak, the other was the component which was revealed on the SGE pattern as two conspicuous bands.Finally, to give one more certainty to this conclusion above, the presence of the bound ADP in the component which is specific to F-actin, was investigated by measuring theabsorbance at 260 mμ through DEAE cellulose column chromatography. The result proved the obvious presence of the bound ADP.
- 鹿児島大学の論文
- 1969-03-25
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