Isolation and structures of alligator gar (Lepisosteus spatula) insulin and pancreatic polypeptide

Autor: Joe R. Kimmel, Valentine A. Lance, J.W. Hamilton, Kurt E. Ebner, Allen B. Rawitch, H.G. Pollock, J.B. Rouse
Rok vydání: 1987
Předmět:
Zdroj: General and Comparative Endocrinology. 67:375-382
ISSN: 0016-6480
DOI: 10.1016/0016-6480(87)90192-4
Popis: Insulin and a 36-residue peptide with homology to pancreatic polypeptide (PP) were isolated from the endocrine pancreas of the alligator gar (Lepisosteus spatula), a ganoid fish, by gel filtration and HPLC. Heterologous radioimmunoassays were used to detect insulin-like and PP-like immunoreactivities during purification of the two peptides. The sequence of the 36-amino acid peptide containing a C-terminal tyrosinamide was identical at 31 of 36 positions to porcine neuropeptide Y (NPY). The amino acid sequence of this peptide is YPPKPENPGEDAPPEELAKYYSALRHYINLITRQRY-NH2. The second peptide, gar insulin, contains 52 amino acid residues and is composed of a 21-residue A chain and a 31-residue B chain. The sequence of the A chain is GIVEQCCHKPCTIYELENYCN. The sequence of the B chain is AANQHLCGSHLVEALYLVCGEKGFFYNPNKV.
Databáze: OpenAIRE