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Connecting Peptide, Correcting Peptide?

Michelle Hoffman
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Copyright ©2004 by the American College of Physicians


Ann Intern Med. 1997;127(12):1147-1148. doi:10.7326/0003-4819-127-12-199712150-00050
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In biochemistry textbooks, insulin is uniformly described as a small protein consisting of two peptide chains held together by disulfide bonds. Initially, the hormone is manufactured as a single precursor molecule called proinsulin, from which a connecting peptide (or C peptide) is later excised, leaving the mature insulin molecule (Figure 1). Most books continue with a description of insulin's role in lowering blood glucose levels and controlling lipolysis in adipose tissue, but C peptide is rarely mentioned again. Indeed, until recently, C peptide was viewed essentially as a waste product that played no role in regulation of metabolism or in the treatment of diabetes.

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peptides ; c-peptide

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Figures

Grahic Jump Location
Figure 1.
C peptide (open circles) is cleaved from proinsulin at the dipeptides (Arg-Arg and Lys-Arg) to produce insulin (filled circles).

Two disulfide bonds connect insulin's A chain, composed of 21 amino acids, and B chain, composed of 30 amino acids. The A chain also contains a third disulfide bond.

Grahic Jump Location

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