Kobayashi K, Hara A, Takano K, Hirai H
Mol Immunol. 1982 Jan;19(1):95-103. doi: 10.1016/0161-5890(82)90251-6.
Immunoglobulin M (IgM) was isolated from serum of the chum salmon (Oncorhynchus keta) by means of ion-exchange chromatography followed by gel filtration. The purified chum salmon IgM had a mol. wt of 730,000 and a tetrameric structure. However, a fraction of tetrameric IgM was considered to be non-covalently associated molecules. The amino acid composition was determined for the chum salmon micro-and L-chains and was found to be similar to that reported for other teleost fish micro- and L-chains. No J-chain- like component could be identified in the salmon IgM by either alkaline urea polyacrylamide gel electrophoresis or by the immunological cross-reaction with antisera to the human and chicken J-chain. The immunoglobulin cross-reactivity between the chum salmon micro-chain and that of 22 other fishes was tested, and only micro-chains from the family Salmonidae revealed cross-reactivity.
通过离子交换色谱法随后进行凝胶过滤，从大麻哈鱼（Oncorhynchus keta）血清中分离出免疫球蛋白M（IgM）。纯化后的大麻哈鱼IgM分子量为730,000，具有四聚体结构。然而，一部分四聚体IgM被认为是非共价结合分子。测定了大麻哈鱼μ链和L链的氨基酸组成，发现其与其他硬骨鱼μ链和L链的报道相似。通过碱性尿素聚丙烯酰胺凝胶电泳或与人及鸡J链抗血清的免疫交叉反应，在鲑鱼IgM中均未鉴定出类似J链的成分。测试了大麻哈鱼μ链与其他22种鱼类μ链之间的免疫球蛋白交叉反应性，只有鲑科鱼类的μ链显示出交叉反应性。
