Open AccessBovine Proinsulin: Amino Acid Sequence of the C‐Peptide Isolated from Pancreas
Author(s) -
Salokangas Anneli,
Smyth Derek G.,
Markussen Jan,
Sundby Finn
Publication year - 1971
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1971.tb01377.x
Subject(s) - proinsulin , papain , peptide , chymotrypsin , peptide sequence , biochemistry , trypsin , protein primary structure , amino acid , digestion (alchemy) , chemistry , biology , enzyme , chromatography , insulin , endocrinology , gene
The amino acid sequence of the proinsulin C‐peptide isolated from bovine pancreas has been determined and the experimental data is presented. Digestion of C‐peptide with chymotrypsin provided three fragments, the compositions of which accounted for the whole structure. Digestion of the three peptides with papain gave rise to a variety of small peptides, which were isolated. The sequences of the chymotrypsin and papain peptides allowed the primary structure of bovine C‐peptide to be assigned. The similarity of the sequence obtained for C‐peptide isolated from bovine pancreas with that written for C‐peptide from bovine proinsulin provides strong evidence for their identity. The sequence presented contains two differences from that cited previously.