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Insulin was extracted and purified from the pancreas of the adult bullfrog, Rana gatesbelana, using Sephadex gel filtration and reverse phase high performance liquid chromatography <HPLC). A porcine insulin radioimmunoassay <RIA) was used to detect insulin immunoreactivity during purification. Twenty-five grams of pancreas tissue yielded 674 ug of pure insulin. Analysis of acid hydrolysates of the pure peptide showed that bullfrog insulin contained 52 amino acids. A and B chains were separated and their amino acid sequences determined. The amino acid sequence of bullfrog insulin is unique when compared to other known insulins. The amino terminus of the A chain has a two amino acid extension, not found in any other known insulin sequence. In addition, a methionine is substituted at B17 for the leucine seen in most mammal insulins. Most of the structurally important amino acids have been conserved, thus preserving the integrity of the three-dimensional molecule. The most notable are the six cysteines, the zinc binding site (BIO, histidine), and nonpolar surface sequences involved in dimerization (B12-B16, B24-B25) and hexamerization CB14, B18, A13, A14).

A novel insulin from the bullfrog: its structure and function in protein secretion by hepatocytes