Abstract
In this communication we report a simple and efficient approach to C-peptide quantitation using isotope dilution mass-spectrometry analysis. The method facilitates quantitation of C-peptide levels at least one order of magnitude lower compared to concentration levels achieved with an IDA method reported previously. The improvement was due to more intensive sample preparation procedure that, in turn, makes it possible to increase the sample load without a corresponding increase in matrix effects. We also show the results of a comparison study with a second laboratory using a similar previously reported method for C-peptide quantitation.
Highlights
C-peptide is a 31-amino acid central part of the pro-insulin molecule
Equal amounts of insulin and C-peptide are released from cleavage of proinsulin by specific beta cell endopeptidases within the pancreatic islets of Langerhans
C-peptide has generally been considered a byproduct of insulin biosynthesis, but recent data suggest that it may have biological significance [1,2,3]
Summary
C-peptide is a 31-amino acid central part of the pro-insulin molecule. Equal amounts of insulin and C-peptide are released from cleavage of proinsulin by specific beta cell endopeptidases within the pancreatic islets of Langerhans. Keywords C-peptide/Mass spectrometry; Isotope dilution assay; Ion Exchange chromatography; Sample preparation The authors used reversed phase chromatography in LC-MS quantitation, and employed solid phase extraction for sample preparation.
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