• Korean Journal of Fisheries and Aquatic Sciences
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• v.5 no.1
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• pp.29-38
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• 1972

The protein composition of abalone muscle was estimated with the following result: on a series of samples analyzed, water-soluble protein, $19\~22\%$, salt-soluble protein, $27\~39\%$: alkali-soluble protein, $20\~26\%$ : and stroma $20\~28\%$ : respectively. It was demonstrated by ultracentrifugal analysis that approximately $65\%$ of the salt-soluble protein is accounted for by paramyosin, $30\%$ by actomyosin, and $5\%$ by myosin, respectively. The ultracentrifugally homogenous paramyosin was prepared by BAILEY's ethanol-dried method. It showed a $S^{\circ}\;_{20,\;{\omega}$ of 3.14s, and was completely salted in with KCl beyond $0.35{\mu}$. The intrinsic viscosity at $25^{\circ}C$ was estimated at 3.1. The paramyosin is rich in several amino acids such as arginine, aspartic acid, glutamic acid, etc., and lacking of both proline and tryptophane, in rough accord with other paramyosins reported. The abalone paramyosin did not show ATPase activity over a pH range of 5 to 9,5 even in the presence of Ca++ or Mg++. So was the case with the paramyosin specimen prepared by BAILEY's wet-extraction method.