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Purification of peptide hormones from chinchilla pancreas by chemical assay.

作者信息

Eng J, Kleinman W A, Chu L S

机构信息

Solomon A. Berson Research Laboratory, Veterans Affairs Medical Center, Bronx, NY 10468.

出版信息

Peptides. 1990 Jul-Aug;11(4):683-5. doi: 10.1016/0196-9781(90)90180-d.

Abstract

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#.

摘要

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