Isolation, primary structure, and biological and immunological properties on pink and chum salmon insulins

• Published in: Comparative biochemistry and physiology. B, Comparative biochemistry Vol. 95; no. 3; pp. 477 - 482
• Main Authors: RUSAKOV, Y. I, KARASEV, V. S, BONDAREVA, V. M, PERTSEVA, M. N, PANKOV, Y. A
• Format: Journal Article
• Language: English
• Published: New York, NY Elsevier Science 1990
• Subjects: Amino Acid Sequence; Animals; Biological and medical sciences; Brackish; Chromatography, Ion Exchange; Crystallization; Endocrine pancreas; Female; Freshwater; Fundamental and applied biological sciences. Psychology; Hormones. Régulation; Insulin - immunology; Insulin - isolation & purification; Insulin - physiology; Male; Marine; Molecular Sequence Data; Oncorhynchus gorbuscha; Oncorhynchus keta; Radioimmunoassay; Salmon - metabolism; Vertebrates: endocrinology; Vertebrata; Antigenic determinant; Molecular structure; Radioimmunoassay; Pisces; Isolation; Oncorhynchus gorbuscha; Oncorhynchus keta; Insulin; Biological activity; Aminoacid sequence
• ISSN: 0305-0491
• DOI: 10.1016/0305-0491(90)90006-F

1. Insulins have been isolated from islet tissue of pink (Oncorhynchus gorbuscha) and chum (Oncorhynchus keta) salmon. The primary structure of chum and pink salmon insulins was found to be identical. Compared to the amino acid sequence of human insulin, the salmon insulins under study differed at 14 positions. 2. Biological activity of pink salmon insulin was 83% of that of standard porcine insulin. 3. The immunological properties of fish insulins were investigated in specific radioimmunoassay (RIA) systems, based on porcine and pink salmon insulins. 4. A significant difference in the antigenic determinants of these fish and mammalian hormones was revealed.