Studies on subunit components of immunoglobulin M from a bony fish, the chum salmon (Oncorhynchus keta)
1982; Elsevier BV; Volume: 19; Issue: 1 Linguagem: Inglês
10.1016/0161-5890(82)90251-6
ISSN1872-9142
AutoresKunihiko Kobayashi, Hara Akihiko, Takano Kazunori, Hirai Hidematsu,
Tópico(s)Glycosylation and Glycoproteins Research
ResumoImmunoglobulin 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 μ-and L-chains and was found to be similar to that reported for other teleost fish μ- 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 μ-chain and that of 22 other fishes was tested, and only μ-chains from the family Salmonidae revealed cross-reactivity.
Referência(s)