Purification of peptide hormones from chinchilla pancreas by chemical assay.
Glucagon was purified from chinchilla pancreas and its biological activity determined. It was isolated using a chemical assay to identify peptides with a histidyl residue at the N-terminus. Chinchilla glucagon has the amino acid sequence HSQGTFTSDYSKHLDSRYAQEFVQWLMNT. It differs from the usual mammalian glucagon by amino acid substitutions at positions 13, 18 and 21 from the N-terminus. Despite these sequence changes, its biological activity is conserved. Chinchilla glucagon has approximately the same potency as pig glucagon in stimulating liver membrane adenyl cyclase activity. Pancreatic polypeptide was also purified from chinchilla pancreas based on its Ala1 signal and has the sequence APLEPVYPGDNATPEQMAQYAAEMRRYINMLTRPRY#.
Eng
J
J
Solomon A. Berson Research Laboratory, Veterans Affairs Medical Center, Bronx, NY 10468.
Kleinman
W A
WA
Chu
L S
LS
D000262:Adenylyl Cyclases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001681:Biological Assay; D002682:Chinchilla / Q000378:metabolism*; D004285:Dogs; D005934:Glucagon / Q000302:isolation & purification*; D066298:In Vitro Techniques; D007328:Insulin / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D010179:Pancreas / Q000737:chemistry*; D010191:Pancreatic Polypeptide / Q000302:isolation & purification*; D012689:Sequence Homology, Nucleic Acid
D007328:Insulin; D010191:Pancreatic Polypeptide; D005934:Glucagon; D000262:Adenylyl Cyclases