Isolation and amino acid sequence of insulins and C-peptides of European bison (Bison bonasus) and fox (Alopex lagopus).
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.
Majewski
T
T
Department of Chemistry, Warsaw University, Poland.
Thim
L
L
Izdebski
J
J
Markussen
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002096:C-Peptide / Q000032:analysis*; D002851:Chromatography, High Pressure Liquid; D005589:Foxes; D007328:Insulin / Q000032:analysis*; D008969:Molecular Sequence Data; D012016:Reference Values; D012418:Ruminants
D002096:C-Peptide; D007328:Insulin