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JBC, Vol. 250, Issue 16, 6288-6290, Aug, 1975

Guinea pig proinsulin. Primary structure of the C-peptide isolated from pancreas

D. E. Massey and D. G. Smyth

The amino acid sequence of the proinsulin C-peptide isolated from guinea pig pancreas was determined and experimental data are presented. Digestion of the C-peptide with chymotrypsin provided two dodecapeptides, a tetrapeptide, and glutamine, which account for the intact chain. Reaction of the C-peptide with cyanogen bromide resulted in cleavage at the single methionine and provided two additional fragments. Digestion of the large peptides with papain provided a variety of small peptides and the complete sequence was assigned by identification of the fragments. Although guinea pig insulin differs markedly from mammalian insulins, guinea pig C-peptide has many features of primary structure in common with the C-peptides of other mammals. The conservation of specific residues in C-peptides indicates that these residues form essential elements in the three-dimensional structure of proinsulin.
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