Isolation and amino acid sequence of insulins and C‐peptides of European bison ( Bison bonasus) and fox ( Alopex lagopus)

• Published in: International Journal of Peptide and Protein Research
• Main Authors: MAJEWSKI, TADEUSZ, THIM, LARS, IZDEBSKI, JAN, MARKUSSEN, JAN
• Format: Article in Journal/Newspaper
• Language: English
• Published: Wiley 1987
• Subjects: Alopex lagopus
• Online Access: http://dx.doi.org/10.1111/j.1399-3011.1987.tb03345.x; https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1399-3011.1987.tb03345.x; https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3011.1987.tb03345.x

Insulins and C‐peptides were extracted and purified from bison and fox pancreatic glands. The insulins were reduced and pyridylethylated, and the derived A‐ and B‐chains separated by HPLC. Amino acid sequence determinations of the pyridylethylated A‐ and B‐chains proved bisontine insulin to be identical to bovine insulin and fox insulin to be identical to dog and porcine insulin. Bisontine C‐peptide proved to be identical to bovine C‐peptide. The isolated fox C‐peptide comprises 23 amino acid residues and probably represents a major tryptic fragment of a larger C‐peptide. The fox C‐peptide fragment is identical to the dog C‐peptide (9–31) except for residue 3 (residue 11 in the dog C‐peptide), which is aspartic acid as compared with glutamic acid in the dog C‐peptide.