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MEDICA 2019 - World Forum for Medicine
Düsseldorf, GermanyBooth No.: 3/D35-2
AACC Annual Scientific Meeting and Clinical Lab Expo
Anaheim Convention Center ~ Anaheim, CABooth No.: 2627
Thanks to Block Scientific, I was able to procure the re-certified Bayer DCA 2000+ without hassles and get the lab back in operation. The
device works perfectly and I look forward to doing more business with Block Scientific.
--- Mathew Anderson, New Jersey
The DRG C-Peptide ELISA is an enzyme immunoassay for the quantitative in vitro diagnostic measurement of CPeptide in serum, plasma and urine.
Insulin is synthesized in the pancreatic beta cells as a 6000 MW component of an 86 amino acid polypeptide called proinsulin (1, 2, 3). Proinsulin is subsequently cleaved enzymatically, releasing insulin into the circulation along with a residual 3000 MW fragment called connection ("C") peptide, so-named because it connects A and B chains of insulin within the proinsulin molecule (1, 2, 3, 4). Human C-Peptide, a 31 amino acid residue peptide, has a molecular mass of
approximately 3000 daltons. C-Peptide has no metabolic function. However, since C-Peptide and insulin are secreted in equimolar amounts, the immunoassay of C-Peptide permits the quantitation of insulin secretion (4, 5, 6). This is the reason for the clinical interest of serum and urinary determinations of C-Peptide. Moreover, C-Peptide measurement has several advantages over immunoassays of insulin.
The half-life of C-Peptide in the circulation is between two and five times longer than that of insulin (7). Therefore, CPeptide levels are a more stable indicator of insulin secretion than the more rapidly changing levels of insulin. A very clear practical advantage of C-Peptide measurement arising from its relative metabolic inertness as compared to insulin is
that C-Peptide levels in peripheral venous blood are about 5-6 times greater than insulin levels (3). Also, relative to an insulin assay, the C-Peptide assay's advantage is its ability to distinguish endogenous from injected insulin.
Thus, low C-Peptide levels are to be expected when insulin is diminished (as in insulin-dependent diabetes) or suppressed (as a normal response to exogenous insulin), whereas elevated C-Peptide levels may result from the increased β-cell activity observed in insulinomas (3, 6, 9).
C-Peptide has also been measured as an additional means for evaluating glucose tolerance and glibenclamide glucose tests (2, 3, 9, 10). C-Peptide levels are in many ways a better measurement of endogenous insulin secretion than peripheral insulin levels. CPeptide may be measured in either blood or urine (9). With improved sensitive C-Peptide immunoassays, it is now possible to measure C-Peptide values at extremely low levels. The clinical indications for C-Peptide measurement include diagnosis of insulinoma and differentation from factitious hypoglycemia, follow-up of pancreatectomy, and evaluation of viability of islet cell transplants (11, 12, 13). Recently, these indications have been dramatically expanded to permit evaluation of insulin dependence in maturity onset diabetes mellitus.