Literature DB >> 2235678

Purification of peptide hormones from chinchilla pancreas by chemical assay.

J Eng1, W A Kleinman, L S Chu.   

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#.

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Year:  1990        PMID: 2235678     DOI: 10.1016/0196-9781(90)90180-d

Source DB:  PubMed          Journal:  Peptides        ISSN: 0196-9781            Impact factor:   3.750


  1 in total

1.  Isolation and amino acid sequences of squirrel monkey (Saimiri sciurea) insulin and glucagon.

Authors:  J H Yu; J Eng; R S Yalow
Journal:  Proc Natl Acad Sci U S A       Date:  1990-12       Impact factor: 11.205

  1 in total

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