Key points are not available for this paper at this time.
Subfragment-1 was isolated from rabbit skeletal muscle myosin by chymotryptic digestion. It was shown by gel electrophoresis in the presence of SDS that this subfragment-1 contained g1-chain and g3-chain, but was lacking in g2-chain. The subfragment-1 migrated as two protein bands on acrylamide-gel electrophoresis under non-dissociating conditions. These two protein components were separated by DEAE-cellulose (DE-32) column chromatography by means of one-step elution using 0.08 M KCl-20 mM TES buffer (pH 7.5). One component contained g1-chain and the other, g3-chain. The Ca-ATPase activity of the former was about one-third of that of the latter.
Yagi et al. (1974) studied this question.