Abstract
PROINSULIN is a single-chain polypeptide in which the A and B chains of insulin are linked together by the connecting peptide1. The terminals of the connecting peptides are occupied by the basic dipeptides, Arg–Arg and Lys–Arg, respectively, and proinsulin C-peptide is defined as connecting peptide minus the basic dipeptides. The immunological reactivity of synthetic [59-formyllysine]-bovine proinsulin 31–60, which comprises the entire sequence of the connecting peptide segment of bovine proinsulin, is indistinguishable from that of natural bovine proinsulin when compared on an equimolar basis2. The immunoassay system involved a bovine proinsulin antiserum3, which was purified by the removal of the antibodies directed towards the insulin region of the molecule. We have now evaluated the structural features of bovine connecting peptide segment which determine its reactivity with bovine proinsulin antisera. For this purpose, homogeneous synthetic peptides of defined structures serve as excellent substrates. We synthesised twelve peptides related to bovine proinsulin C-peptide which has the following amino acid sequence
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YANAIHARA, N., SAKURA, N., YANAIHARA, C. et al. Syntheses and immunological evaluation of bovine proinsulin C-peptide analogues. Nature 258, 365–366 (1975). https://doi.org/10.1038/258365a0
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DOI: https://doi.org/10.1038/258365a0
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