Evaluation of protein quantification using standard peptides containing single conservative amino acid replacements

10Citations
Citations of this article
25Readers
Mendeley users who have this article in their library.

Abstract

Structural analogs are evaluated as peptide internal standards for protein quantification with liquid chromatography-multiple reaction monitoring mass spectrometry (LC-MRM); specifically, single conservative amino acid replacements (SCAR) are performed to create tagged standards that differ by the addition or subtraction of a single methylene group in one amino acid side chain. Because the performance of stable isotope-labeled standards (SIS) has been shown to be superior to structural analogs, differences in both development and quantitative performance between assays based on SIS and SCAR peptides are explored. To establish an assay using the structural analogs, analysis of endogenous, SCAR and SIS peptides was performed to examine their ion signal, fragmentation patterns and response in LC-MRM. Performance of SCAR and SIS peptides was compared for quantification of epidermal growth factor receptor from lung cancer cell lysates and immunoglobulin M in the serum of multiple myeloma patients. © 2012 John Wiley & Sons, Ltd.

Cite

CITATION STYLE

APA

Remily-Wood, E. R., & Koomen, J. M. (2012). Evaluation of protein quantification using standard peptides containing single conservative amino acid replacements. Journal of Mass Spectrometry, 47(2), 188–194. https://doi.org/10.1002/jms.2053

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free