Analytical development of seamless procedures on cation-exchange chromatography and ion-pair chromatography with high-precision mass spectrometry for short-chain peptides

Takano, Yoshinori; Oba, Yasuhiro; Furota, Satoshi; Naraoka, Hiroshi; Ogawa, Nanako O.; Blattmann, Thomas M.; Ohkouchi, Naohiko

doi:10.1016/j.ijms.2021.116529

Cited by 6 publications

(6 citation statements)

References 75 publications

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“…The solution was dried, and AAs were redissolved in 0.5 ml of 0.1M HCl. The consistency of the δ 13 C and δ 15 N compositions of underivatized AAs during the resin treatment has been reported previously 50,52 …”

Section: Methodssupporting

confidence: 78%

“…The stationary phase of the Hypercarb column consists of porous graphitic carbon, which causes a unique and complex retention mechanism 47,48 . This column has been applied to the identification and quantification of AAs and short peptides in natural samples 49–52 . In this research, we have successfully developed a new method, applying the Hypercarb column to δ 13 C and δ 15 N analyses of AAs.…”

Section: Introductionmentioning

confidence: 99%

“…47,48 This column has been applied to the identification and quantification of AAs and short peptides in natural samples. [49][50][51][52] In this research, we have successfully developed a new method, applying the Hypercarb column to δ 13 C and δ 15 N analyses of AAs. The separation performance of hydrophilic AAs using this column was carefully evaluated.…”

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confidence: 99%

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Application of a porous graphitic carbon column to carbon and nitrogen isotope analysis of underivatized individual amino acids using high‐performance liquid chromatography coupled with elemental analyzer/isotope ratio mass spectrometry

Sun

Ogawa

Ishikawa

et al. 2023

Rapid Comm Mass Spectrometry

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RationaleIsolation of underivatized amino acids (AAs) using high‐performance liquid chromatography (HPLC) is becoming a popular method for carbon (δ13C) and nitrogen isotope (δ15N) analyses of AAs because of the high analytical precision and for performing dual‐isotope analysis. However, some AAs in natural samples, especially small, hydrophilic AAs, are not suitably separated using reversed‐phase columns (e.g., C18) and ion‐exchange columns (e.g., Primesep A).MethodsWe developed a new method for HPLC using a porous graphitic carbon column for the separation of nine hydrophilic AAs. After purification, δ13C and δ15N values of AAs were determined using elemental analyzer/isotope ratio mass spectrometry (EA/IRMS). We demonstrated the application of this method by determining δ13C and δ15N values of individual hydrophilic AAs in a biological sample, the muscle of blue mackerel (Scomber australasicus).ResultsChromatographically, the baseline separation of hydrophilic AAs was achieved in both the standard mixture and the biological sample. We confirmed that δ13C and δ15N values of AA standards remained unchanged during the whole experimental procedure. The δ13C values of AAs in mackerel muscle are also in good agreement with the values obtained using another verified method for δ13C analysis.ConclusionsThe good separation performance of hydrophilic AAs and the reliability of δ13C and δ15N analyses of individual AAs using the porous graphite column offer a significant advantage over conventional settings. We suggest that, in the future, the HPLC × EA/IRMS method can be used for reliable δ13C and δ15N analyses of AAs in natural samples.

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Section: Methodssupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

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Application of a porous graphitic carbon column to carbon and nitrogen isotope analysis of underivatized individual amino acids using high‐performance liquid chromatography coupled with elemental analyzer/isotope ratio mass spectrometry

Sun

Ogawa

Ishikawa

et al. 2023

Rapid Comm Mass Spectrometry

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“…45 IEC uses electrostatic interaction to separate peptides. 46,47 The most obvious advantage is that the separation conditions are closest to the biological physiological environment and can maintain the biological activity of the peptides. 48,49 SEC is mainly used in the fractional analysis of the molecular weight of peptides and the determination of the relative molecular mass distribution and is the preferred method for the separation and purification of mixed peptides.…”

Section: Recent Developments Of Lc-msmentioning

confidence: 99%

“…Its separation speed and efficiency are better than other HPLC models 45 . IEC uses electrostatic interaction to separate peptides 46,47 . The most obvious advantage is that the separation conditions are closest to the biological physiological environment and can maintain the biological activity of the peptides 48,49 .…”

Section: Recent Developments Of Lc–msmentioning

confidence: 99%

Application of peptide biomarkers in life analysis based on liquid chromatography–mass spectrometry technology

Han

Cong

et al. 2022

BioFactors

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Biomedicine is developing rapidly in the 21st century. Among them, the qualitative and quantitative analysis of peptide biomarkers is of considerable importance for the diagnosis and therapy of diseases and the quality evaluation of drugs and food. The identification and quantitative analysis of peptides have been going on for decades. Traditionally, immunoassays or biological assays are generally used to quantify peptides in biological matrices. However, the selectivity and sensitivity of these methods cannot meet the requirements of the application. The separation and analysis technique of liquid chromatography-mass spectrometry (LC-MS) supplies a reliable alternative. In contrast to immunoassays, LC-MS methods are capable of providing the analytical prowess necessary to satisfy the demands of peptide biomarker research in the life sciences arena. This review article provides a historical account of the in-roads made by LC-MS technology for the detection of peptide biomarkers in the past 10 years, with the focus on the qualification/quantification developments and their applications.

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Analysis of human biological samples using porous graphitic carbon columns and liquid chromatography-mass spectrometry: a review

Rodrigues,

Cunha,

Barci

et al. 2024

Anal Bioanal Chem

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Analytical development of seamless procedures on cation-exchange chromatography and ion-pair chromatography with high-precision mass spectrometry for short-chain peptides

Cited by 6 publications

References 75 publications

Application of a porous graphitic carbon column to carbon and nitrogen isotope analysis of underivatized individual amino acids using high‐performance liquid chromatography coupled with elemental analyzer/isotope ratio mass spectrometry

Application of a porous graphitic carbon column to carbon and nitrogen isotope analysis of underivatized individual amino acids using high‐performance liquid chromatography coupled with elemental analyzer/isotope ratio mass spectrometry

Application of peptide biomarkers in life analysis based on liquid chromatography–mass spectrometry technology

Analysis of human biological samples using porous graphitic carbon columns and liquid chromatography-mass spectrometry: a review

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