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Human C-Peptide has a molecular mass of approximately 3000 daltons. C-Peptide has no metabolicfunction. However, since C-Peptide and insulin are secreted in equimolar amounts, the immunoassay of CPeptide permits the quantitation of insulin secretion. This is the reason for the clinical interest of serum orplasma determinations of C-Peptide. Moreover, C-Peptide measurement has several advantages overimmunoassays of insulin. The half-life of C-Peptide in the circulation is between two and five times longerthan that of insulin. Therefore, C-Peptide levels are a more stable indicator of insulin secretion than themore rapidly changing levels of insulin. A very clear practical advantage of C-Peptide measurement arisingfrom its relative metabolic inertness as compared to insulin is that C-Peptide levels in peripheral venousblood are about 5-6 times greater than insulin levels. Also, relative to an insulin assay, the C-Peptideassay's advantage is its ability to distinguish endogenous from injected insulin. C-Peptide has also beenmeasured as an additional means for evaluating glucose tolerance and glibenclamide glucose tests. CPeptide levels are in many ways a better measurement of endogenous insulin secretion than peripheralinsulin levels. C-Peptide may be measured in either blood or urine. With improved sensitive C-Peptideimmunoassays, it is now possible to measure C-Peptide values at extremely low levels. The clinicalindications for C-Peptide measurement include diagnosis of insulinoma and differentiation from factitioushypoglycemia, follow-up of pancreatectomy, and evaluation of viability of islet cell transplants. Recently,these indications have been dramatically expanded to permit evaluation of insulin dependence in maturityonset diabetes mellitus.