Primary structure of insulin and glucagon from the flounder (Platichthys flesus).
Insulin and glucagon have been isolated from the Brockmann bodies of the flounder, a teleostean fish, and their primary structures established by automated Edman degradation. The A-chain of flounder insulin shows strong homology to the A-chains from the coho salmon (Oncorhynchus kisutch; 100%) and the anglerfish (Lophius americanus; 95%) but homologies in the B-chain region are weaker (salmon 79%, anglerfish 83%). Flounder insulin B-chain contains the novel sequence Val-Val-Pro-Pro at the NH2 terminus and the highly conserved seryl residue at position 10 (B 9 in mammals) is replaced by an alanyl residue. Flounder glucagon is identical to anglerfish glucagon II but shows four amino acid substitutions compared with salmon glucagon.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005412:Flatfishes / Q000502:physiology*; D005432:Flounder / Q000502:physiology*; D005934:Glucagon / Q000032:analysis* / Q000302:isolation & purification; D007328:Insulin / Q000032:analysis* / Q000302:isolation & purification; D011863:Radioimmunoassay
D000596:Amino Acids; D007328:Insulin; D005934:Glucagon