1972 年 38 巻 2 号 p. 126-132
The chromatography of carp myosin prepared by the method described previously was carried out on DEAE-Sephadex A-50 according to the procedure of RICHARDS et al. (1967).
The elution profiles of carp myosin at 280 mμ were very similar to those of myosins obtained from rabbit, chicken, and tuna already reported. It was therefore confirmed that carp myosin was found to consist mainly of monomeric myosin.
The specific ATP-ase activity of the main peak was approximately 50-90% higher than that of the original myosin and the absorbance ratio at 280 mμ to that at 260 mμ also increased from 1.25 of the original to 1.95 of the chromatographed myosin.
No adenylic deaminase activity was found in the main myosin peak.
It was clear that considerable purification of carp myosin was achieved by this procedure.