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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Remily-Wood, Elizabeth R. Koomen, John M.
Description	Country affiliation: United States Author Affiliation: Remily-Wood ER ( Molecular Oncology and Proteomics, H. Lee Moffitt Cancer Center & Research Institute, University of South Florida, Tampa, FL 33612, USA.)
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.
File Format	HTM / HTML
ISSN	10765174
e-ISSN	10969888
DOI	10.1002/jms.2053
Journal	Journal of Mass Spectrometry
Issue Number	2
Volume Number	47
Language	English
Publisher	Wiley
Publisher Date	2012-02-01
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Discipline Spectroscopy Discipline Chemistry Techniques Mass Spectrometry Peptides Proteins Amino Acid Substitution Amino Acids Chemistry Cell Line, Tumor Immunoglobulin M Blood Lung Neoplasms Metabolism Multiple Myeloma Receptor, Epidermal Growth Factor Reference Standards Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s.
Content Type	Text
Resource Type	Article
Subject	Spectroscopy Medicine

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Quantification of peptides from immunoglobulin constant and variable regions by LC-MRM MS for assessment of multiple myeloma patients.

Utilization of a deuterated derivatization agent to synthesize internal standards for gas chromatography-tandem mass spectrometry quantification of silylated metabolites.

Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains.

Identification of isomeric 5-hydroxytryptophan- and oxindolylalanine-containing peptides by mass spectrometry.

An improved chemical approach toward the C-terminal sequence analysis of proteins containing all natural amino acids.

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Recombinant thiopeptides containing noncanonical amino acids.

Specific rearrangement reactions of acetylated lysine containing peptide bn (n = 4-7) ion series.

Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution.

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

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Quantification of peptides from immunoglobulin constant and variable regions by LC-MRM MS for assessment of multiple myeloma patients.

Utilization of a deuterated derivatization agent to synthesize internal standards for gas chromatography-tandem mass spectrometry quantification of silylated metabolites.

Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains.

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