SDS存在下におけるコイ筋原繊維たんぱく質のゲル〓過と電気泳動

概要

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A gel filtration method in the presence of sodium dodecyl sulfate (SDS) was applied to the separation of the components of myofibrillar proteins from fish muscle. A characterization of the components obtained by gel filtration chromatography was made by measuring the mobilities on SDS-polyacrylamide gel electrophoresis.Gel filtration of carp myosin gave two clearly separated peaks, corresponding to myosin heavy chains and light chains. The weight ratio of heavy chains to light chains of myosin was estimated to be approximately 87:13, while carp actin gave a single peak which was eluted between the peaks of myosin heavy chains and light chains.Actomyosin was separated into three peaks. The weight ratio of myosin to actin in actomyosin prepared by the ordinary method was estimated to be approximately 3:1.Myofibrils, accounting for 70% of the muscle proteins, were completely dissolved in SDS. The elution pattern of dissolved myofibrils was closely similar to that of actomyosin.The present method was successfully used to examine the purity of myosin, actin, and actomyosin and to estimate the contents of their respective components.
日本水産學會の論文