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Development of a derivatisation method for the analysis of aldehyde modified amino acid residues in proteins by Fourier transform mass spectrometry

Pournamdari, M. and Saadi, Ahmed and Ellis, E. and Andrew, Ruth and Walker, Brian and Watson, D.G. (2009) Development of a derivatisation method for the analysis of aldehyde modified amino acid residues in proteins by Fourier transform mass spectrometry. Analytica Chimica Acta, 633 (2). pp. 216-222. ISSN 0003-2670

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Abstract

A method was developed for the analysis of amino acids within bovine serum albumin (BSA) which had been modified by reaction with different enals. BSA was reacted with the aldehydes and the reaction products were stabilised by reaction with NaBH4. The protein was then hydrolysed with 6N HCl and the hydrolysis products were analysed by liquid chromatography-mass spectrometry (LC-MS). The modified amino acids were derivatised with propylchloroformate. High resolution mass spectrometry carried out using an LTQ-Orbitrap instrument which was able to characterise a wide range of adducts. In addition double adducts were observed to be formed with 4-hydroxynonenal (HNE) and lysine or lysine + histidine. Qualitatively it was possible to consistently observe a pyridinium adduct formed between lysine and pentenal in human plasma from normal subjects.

Item type: Article
ID code: 13184
Keywords: aldehyde, protein, adduct, fourier transform mass spectrometry, human plasma, pharmacology, Therapeutics. Pharmacology, Pharmacy and materia medica, Microbiology
Subjects: Medicine > Therapeutics. Pharmacology
Medicine > Pharmacy and materia medica
Science > Microbiology
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Related URLs:
    Depositing user: Ms Ann Barker-Myles
    Date Deposited: 12 Oct 2009 12:26
    Last modified: 12 Mar 2012 10:56
    URI: http://strathprints.strath.ac.uk/id/eprint/13184

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