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Study of posttranslational non-enzymatic modifications of collagen using capillary electrophoresis/mass spectrometry and high performance liquid chromatography/mass spectrometry

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Title: Study of posttranslational non-enzymatic modifications of collagen using capillary electrophoresis/mass spectrometry and high performance liquid chromatography/mass spectrometry
Authors: Mikulíková, Kateřina1,2 mikulikova@biomed.cas.cz, Eckhardt, Adam1,3, Pataridis, Statis1, Mikšík, Ivan1,3
Source: Journal of Chromatography A. Jul2007, Vol. 1155 Issue 2, p125-133. 9p.
Subjects: Connective tissues, Extracellular matrix proteins, Biomolecules, Biological products
Abstract: Abstract: The depository effects that occur in slowly metabolized proteins (typically glycation) are very difficult to assess, owing to their extremely low concentration in the protein matrix. Collagen accumulates reactive metabolites through reactions that are not regulated by enzymes. A typical example of these non-enzymatic changes is glycation (the Maillard reaction, the formation of advanced glycation end products), resulting from the reaction of the oxo-group of sugars with the ɛ-amino group of lysine and arginine. Collagen samples (type I) as a test protein were incubated separately with glucose, ribose and malondialdehyde. Collagen was fragmented with cyanogen bromide and then digested with trypsin. This peptide digest was separated by CE, CE–MS/MS, and HPLC–MS/MS. An ion trap MS was used and MS conditions were optimized for both methods. These on-line CE–MS/MS and HPLC–MS/MS couplings made it possible to discover specific modifications such as (N ɛ-(carboxymethyl)-lysine) in the precise location in the structure of collagen corresponding to posttranslational non-enzymatic modifications. A new CE–MS/MS technique for peptide analysis was developed, and applied in the identification of posttranslational modifications in slowly metabolized test proteins. [Copyright &y& Elsevier]
Copyright of Journal of Chromatography A is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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Header DbId: egs
DbLabel: Engineering Source
An: 25411350
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PubTypeId: academicJournal
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  Data: Study of posttranslational non-enzymatic modifications of collagen using capillary electrophoresis/mass spectrometry and high performance liquid chromatography/mass spectrometry
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  Data: <searchLink fieldCode="AR" term="%22Mikulíková%2C+Kateřina%22">Mikulíková, Kateřina</searchLink><relatesTo>1,2</relatesTo><i> mikulikova@biomed.cas.cz</i><br /><searchLink fieldCode="AR" term="%22Eckhardt%2C+Adam%22">Eckhardt, Adam</searchLink><relatesTo>1,3</relatesTo><br /><searchLink fieldCode="AR" term="%22Pataridis%2C+Statis%22">Pataridis, Statis</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Mikšík%2C+Ivan%22">Mikšík, Ivan</searchLink><relatesTo>1,3</relatesTo>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+Chromatography+A%22">Journal of Chromatography A</searchLink>. Jul2007, Vol. 1155 Issue 2, p125-133. 9p.
– Name: Subject
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  Data: <searchLink fieldCode="DE" term="%22Connective+tissues%22">Connective tissues</searchLink><br /><searchLink fieldCode="DE" term="%22Extracellular+matrix+proteins%22">Extracellular matrix proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Biomolecules%22">Biomolecules</searchLink><br /><searchLink fieldCode="DE" term="%22Biological+products%22">Biological products</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Abstract: The depository effects that occur in slowly metabolized proteins (typically glycation) are very difficult to assess, owing to their extremely low concentration in the protein matrix. Collagen accumulates reactive metabolites through reactions that are not regulated by enzymes. A typical example of these non-enzymatic changes is glycation (the Maillard reaction, the formation of advanced glycation end products), resulting from the reaction of the oxo-group of sugars with the ɛ-amino group of lysine and arginine. Collagen samples (type I) as a test protein were incubated separately with glucose, ribose and malondialdehyde. Collagen was fragmented with cyanogen bromide and then digested with trypsin. This peptide digest was separated by CE, CE–MS/MS, and HPLC–MS/MS. An ion trap MS was used and MS conditions were optimized for both methods. These on-line CE–MS/MS and HPLC–MS/MS couplings made it possible to discover specific modifications such as (N ɛ-(carboxymethyl)-lysine) in the precise location in the structure of collagen corresponding to posttranslational non-enzymatic modifications. A new CE–MS/MS technique for peptide analysis was developed, and applied in the identification of posttranslational modifications in slowly metabolized test proteins. [Copyright &y& Elsevier]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Journal of Chromatography A is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1016/j.chroma.2007.01.020
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      – Code: eng
        Text: English
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    Subjects:
      – SubjectFull: Connective tissues
        Type: general
      – SubjectFull: Extracellular matrix proteins
        Type: general
      – SubjectFull: Biomolecules
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      – SubjectFull: Biological products
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      – TitleFull: Study of posttranslational non-enzymatic modifications of collagen using capillary electrophoresis/mass spectrometry and high performance liquid chromatography/mass spectrometry
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            NameFull: Eckhardt, Adam
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            NameFull: Pataridis, Statis
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            NameFull: Mikšík, Ivan
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            – D: 06
              M: 07
              Text: Jul2007
              Type: published
              Y: 2007
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            – TitleFull: Journal of Chromatography A
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