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 mammal...
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Veröffentlicht in: | Peptides (New York, N.Y. : 1980) N.Y. : 1980), 1990-07, Vol.11 (4), p.683-685 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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 Ala
1 signal and has the sequence
APLEPVYPGDNATPEQMAQYAAEMRRYINMLTRPRY# |
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ISSN: | 0196-9781 1873-5169 |
DOI: | 10.1016/0196-9781(90)90180-D |