Abstract
The muscle of abalone was analyzed for protein composition with the following results: water-soluble protein, 22 %; salt-soluble protein, 34%; alkali-soluble protein, 20%; and stroma, 24%. On sedimentation analysis, approximately 65% of the salt-soluble protein was accounted for by paramyosin. An ultracentrifugally homogeneous paramyosin was prepared essentially according to BAILEY's ethanol-dried method. It showed a s020, W of 3.14 S and was completely salted in with KCI beyond 0.35μ. The intrinsic viscosity at 25°C was estimated at 3.1dl/g. The paramyosin was rich in arginine, aspartic acid, and glutamic acid, but did not contain proline or tryptophan, in rough accord with previous reports on other paramyosins. The abalone paramyosin showed little ATPase activity over the pH range examined, 5 through 9.5, irrespective of the presence of Ca++ or Mg++. This was also the case with the paramyosin prepared by a slightly modified BAILEY's wet-extraction method.
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