Latest developments in sample treatment for 18O-isotopic labeling for proteomics mass spectrometry-based approaches: A critical review

Capelo, J.L.; Carreira, Ricardo J.; Fernandes, Luz; Lodeiro, Carlos; Santos, Hugo M.; Simal-Gándara, Jesús

doi:10.1016/j.talanta.2009.04.053

Cited by 49 publications

(78 citation statements)

References 33 publications

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“…The differences are most pronounced in the HCl-decalcified/gelatinized samples (relative to nongelatinized, EDTA-decalcified collagens). The difference among the collagen/gelatin preparations within each sample likely results from oxygen addition and equilibration that is a necessary consequence of partial hydrolysis and carboxyl exchange at low pH (see Capelo et al 2010). The measurement of oxygen isotopic values in gelatin could serve as a monitor of peptide bond breakage as part of the preparation.…”

Section: Resultsmentioning

confidence: 99%

Comparative Decalcification Methods, Radiocarbon Dates, and Stable Isotopes of the VIRI Bones

Tuross¹

2012

Radiocarbon

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ABSTRACT. The Fifth International Radiocarbon Comparison (VIRI) provided a suite of 5 bone samples with consensus ages ranging from 969 to 39,305 14 C yr BP (Scott et al. 2010). These bones were used herein in a comparison of decalcification methods using either HCl or EDTA to produce collagen, and the results demonstrate age concordance between both preparation methods and the VIRI consensus values. Additional isotopic analyses of the collagen (ô l3 C, δ 15 Ν, and δ 18 0) illustrate the increasing sensitivity of carbon, nitrogen, and oxygen isotopes in assessing gelatin degradation.

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Section: Resultsmentioning

confidence: 99%

Comparative Decalcification Methods, Radiocarbon Dates, and Stable Isotopes of the VIRI Bones

Tuross¹

2012

Radiocarbon

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“…The advantages of 18 O enzymatic labeling are: the fact that virtually all the produced peptides are labeled and co-elute with the correspondent unlabeled peptide; the only reagent specifically required is H 2 18 O; and the procedure is easy to adapt in any proteomics lab [15,16]. On the other hand, the procedure is labor-intensive and time-consuming; the labeling efficiency is influenced by many factors (such as pH, enzyme to be used, or the characteristics of the proteins and the peptides); and also if the 18 O-water to be used is less than 95% pure, some of the peptides will be labeled with only one 18 O, resulting in a mass spectra with both 2 Da and m/z O.…”

Section: O Enzymatic Labeling Of Peptidesmentioning

confidence: 99%

“…D) Representation of the iTRAQ 8-plex molecule and the spectra obtained in an iTRAQ experiment with the MS/MS spectrum that is used for identification and a zoom of the low m/z region where the reporter ions are used for quantification. 4 Da mass shifts [15]. Finally, the naturally abundant isotopes may also contribute to the peak intensities making the spectra very complex to analyze and adding the necessity for improved software for data processing [16].…”

Section: O Enzymatic Labeling Of Peptidesmentioning

confidence: 99%

Neuroproteomics — LC-MS Quantitative Approaches

Santa¹,

Anjo²,

Mendes³

et al. 2015

Recent Advances in Proteomics Research

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Neuroproteomics is a scientific field that aims to study all the proteins of the central nervous system, their expression, function, and interactions. The central nervous system is intricate and heterogeneous, and the study of its proteome is consequently complex, with many biological questions still requiring deep investigation. For this, mass spectrometry approaches, most often coupled with liquid chromatography (LC-MS), have been the number one choice in proteomics, and over the years it has added many important findings to the field. At this point it is important that proteomics turns to the quantitative expression of proteins instead of only identifying which proteins are present in a given sample, much because the most important alterations may be slight alterations in the quantity of a protein in a given situation. Therefore, many LC-MS quantitative approaches have been developed relying on the labeling of the proteins or even by using label-free techniques.In this chapter, a brief description of the principles and procedures of several approaches used for relative and absolute, targeted and untargeted quantification of proteins is presented, complemented with a literature revision of their application in the neurosciences field.

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“…Several ways of protein quantitation have been suggested and they can be divided into two main categories; the isotope based and the label free methods. Two papers which give good overviews over the different labeling methods have been published recently (Capelo et al 2010;Vaudel et al 2010). In brief; the main modern strategies for isotopic labeling are divided into metabolic labeling at cell growth called SILAC, chemical labeling at protein level, called iCAT, enzymatic labeling at peptide level, after protein digestion like iTRAQ and labeling during protein digestion, such as 18 O labeling (Capelo et al 2010).…”

mentioning

confidence: 99%

“…Two papers which give good overviews over the different labeling methods have been published recently (Capelo et al 2010;Vaudel et al 2010). In brief; the main modern strategies for isotopic labeling are divided into metabolic labeling at cell growth called SILAC, chemical labeling at protein level, called iCAT, enzymatic labeling at peptide level, after protein digestion like iTRAQ and labeling during protein digestion, such as 18 O labeling (Capelo et al 2010). SILAC can only be used for samples which are produced using labeled amino acids, while the other methods can be used for all types of protein samples.…”

mentioning

confidence: 99%