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利用ProteinA sepharose亲和柱层析一步法,首次分离纯化了4种海水养殖鱼类(3种暖水性鱼类:紫红笛鲷Lutjanusargentimaculatus、青石斑鱼Epinephelusawoara、尖吻鲈Latescal carifer和1种冷水性鱼类牙鲆Paralichthysolivaceus)血清中的免疫球蛋白(Ig)。3种暖水性鱼类Ig的分离效果较好,牙鲆较差。层析曲线的洗脱峰值说明牙鲆血清的Ig同紫红笛鲷、青石斑鱼、尖吻鲈3种暖水性鱼类血清的Ig在结构和功能上有明显的差异。通过SDS PAGE电泳测得其重链分子量分别为紫红笛鲷79.5kDa和75.0kDa、青石斑鱼77.2kDa、尖吻鲈81.8kDa和75.7kDa,牙鲆73.5kDa;轻链分子量分别为30.1kDa、31.1kDa、29.7kDa和15.0kDa。
Four species of marine fish (three species of warm water fish: Lutjanusargentimaculatus, Epinephelusawoara, Latescal carifer and 1 cold-water fish) were isolated and purified by ProteinA sepharose affinity column chromatography. Paralichthys olivaceus Paralichthys olivaceus) serum immunoglobulin (Ig). Isolation of three kinds of warm water fish Ig is better, flounder is poor. The elution peak of chromatogram shows that there is a significant difference in structure and function between the Ig of serum of Japanese flounder with the Ig warm sera of fish of red snapper, blue grouper and barramundi. SDS-PAGE electrophoresis showed that the heavy chain molecular weights were 79.5 kDa and 75.0 kDa respectively, 77.2 kDa for blue grouper, 81.8 kDa and 75.7 kDa for blue grouper, 73.5 kDa for Japanese flounder, and the molecular weights of light chain were 30.1 kDa and 31.1 kDa, 29.7 kDa and 15.0 kDa.