We investigated the changes in protein and free amino acid compositions of the muscles, and amino acid composition of the muscle proteins during postmortem storage of dorsal white and lateral dark muscles of Yellowtail, Seriola quinqueradita, which were kept at $2^{\circ}C$. We present an extensive discussion on the relationship between the changes of freshness and those of protein compositions in the white and the dark muscle of the red-fleshed fish by analyzing polyacrylamide gel electrophoretograms of $NaDodSO_4-solubilized$ sarcoplasmic and myofibrillar proteins extracted from the both muscles. By assessing K-value, total volatile basic nitrogen and pH value as a criterion of freshness, we found that the dark muscle undergoes a more rapid decrease in its freshness compared to that of the white muscle. The contents of the sarcoplasmic and the myofibrillar protein were decreased with postmortem aging of the muscles while those of the residual intracellular protein were increased, and these changes were somewhat faster in the dark muscle than in the white muscle. From the analysis of the electrophoretograms and their densitograms, we found that the sarcoplasmic proteins of the white and the dark muscle were respectively composed of 16 and 12 components. The sarcoplasmic protein of the white muscle lapsed for 10 days showed an increase of 18,000 and 41,000 dalton components, and a gradual decrease of 23,000 and 23,500 dalton components, whereas the sarcoplasmic protein of the dark muscle lapsed for 9 days showed a decrease of 49,000 dalton component, an appearence of a newly formed component of 47,000 dalton, and a disappearance of 26,000 dalton component. The electrophoretograms of the myofibrillar proteins shelved that the white and the dark muscle were composed of 17 and 16 components, respectively. Depending on the lapsed time of postmortem under the controlled condition, the myofibrillar proteins of the white muscle showed an increase of 40,000 dalton component, a gradual decrease of 37,500 dalton component, an appearance of a newly forming component of 32,000 dalton and a disappearance of 26,000 dalton component. On the other hand, the myofibrillar proteins of the dark muscle showed an increase of 58,000 and 64,000 dalton bands, a disappearance of light chain-2 protein and an appearance of a newly forming protein of 32,000 dalton. These changes on the electrophoretic patterns in the dark muscle were more rapid than those in the white muscle. In almost all of the cases, we observed that the changes in the sarcoplasmic protein were faster than those in the myofibrillar protein. The analysis of amino acid of the both muscle proteins showed that the white muscle was rich in glutamic acid, aspartic acid, leucine, arginine, lysine, etc. but was poor in proline and tryptophan. No significant difference was found in the amino acid composition of protein of both the white and the dark muscles. The sample of white muscle lapsed for 10 days shows a remarkable decrease in glutamic and aspartic acids, while that of the dark muscle lapsed for 9 days shows an appreciable decrease in alanine, glycine and arginine. The free amino acid compositions of the white and the dark muscles are respectively characterized with $63\%$ of histidine and $67\%$ of taurine with respect to the total free amino acids of the yellowtail at-death, respectively. The white muscle lapsed for 10 days showed an increase of histidine, valine and taurine, and a slight decrease of alanine, leucine and glycine. The dark muscle lapsed for 9 days shelved an increase of taurine, phenylalanine and glycine, and a decrease of histidine, alanine and serine.