1969 年 35 巻 6 号 p. 555-558
In the previous paper1) it was reported that several peaks of eluted proteins were observed in the elution diagrams of fish muscle protein by gel filtration on agarose gels. To interpret the elution profiles of fish muscle protein, gel filtrations on Sepharose 2B were carried out on sarcoplasmic protein, myosin and actomyosin prepared from fish muscle and also on myosin from rabbit muscle. In the obtained elution patterns, peaks of major compon-ent protein were observed at each definite elution volume (Figs. 1 and 2). Their Kav values were 0.9-1.0 for sarcoplasmic protein, 0.4-0.5 for myosin and 0.0-0.1 for actomyosin (Table 1). These results suggest that fish muscle protein can be fractionated into three kinds of proteins, sarcoplasmic protein, myosin and actomyosin (and/or aggregated protein) by gel filtration on Sepharose 2B.