コガネガレイ筋肉のジェリー化ならびにプロテアーゼ活性と,粘液胞子虫との関連

概要

論文の詳細を見る
Numerous spores of a myxosporidian parasite, tentatively classified as the genus Kudoa, were found in many of the muscle spcimens of the yellowfin sole Limanda aspera which were caught in the Bering Sea. The muscle infected heavily with the parasite, displayed a considerably high protease activity. Such muscle was observed to be easily jellified when left standing at room temperature. Two types of protease occurred in the heavily infected muscle, one designated protease A hydrolyzing hemoglobin optimally at PH 3 and the other designated protease B casein optimally at PH 6.5 under the conditions applied. Protease B activity was not always detected in less infected muscles. The muscle containing both proteases was jellified very rapidly. Both protease activities were strongly inhibited by Hg+2, PCMB or leupeptin, indicating them to be of thiol enzyme. It was concluded from these results that the proteases were produced by the parasite and responsible for the jellification of the muscle.