Insulin has been isolated from islet tissue of coho salmon (Oncorhynchus kisutch) by gel filtration and HPLC and the complete amino acid sequence has been determined. The sequence differs from bovine insulin at 14 sites but all interchanges are conservative from the viewpoint of preservation of conformation. A comparison of insulin sequences from other fish is presented. Salmon insulin cross-reacts very weakly with antiserum to bovine insulin and vice versa. A completely homologous radioimmunoassay has been developed and used to estimate the insulin in salmon islet tissue and in plasma. The hypoglycemic effect of salmon insulin in salmon was more pronounced and persisted longer than that caused by identical doses of bovine insulin.
