PURIFICATION OF PEPTIDE-HORMONES FROM CHINCHILLA PANCREAS BY CHEMICAL-ASSAY

被引:11
作者
ENG, J [1 ]
KLEINMAN, WA [1 ]
CHU, LS [1 ]
机构
[1] CUNY MT SINAI SCH MED,NEW YORK,NY 10029
关键词
Amino acid sequence; Chemical assay; Chinchilla; Glucagon; Pancreatic polypeptide; Purification;
D O I
10.1016/0196-9781(90)90180-D
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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#. © 1990.
引用
收藏
页码:683 / 685
页数:3
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