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.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Journal of Chromatography & Separation Techniques
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
