Skip to content Skip to navigation
University of Warwick
  • Study
  • |
  • Research
  • |
  • Business
  • |
  • Alumni
  • |
  • News
  • |
  • About

University of Warwick
Publications service & WRAP

Highlight your research

  • WRAP
    • Home
    • Search WRAP
    • Browse by Warwick Author
    • Browse WRAP by Year
    • Browse WRAP by Subject
    • Browse WRAP by Department
    • Browse WRAP by Funder
    • Browse Theses by Department
  • Publications Service
    • Home
    • Search Publications Service
    • Browse by Warwick Author
    • Browse Publications service by Year
    • Browse Publications service by Subject
    • Browse Publications service by Department
    • Browse Publications service by Funder
  • Help & Advice
University of Warwick

The Library

  • Login
  • Admin

Determination of types and binding sites of advanced glycation end products for substance P

Tools
- Tools
+ Tools

Lopez-Clavijo, Andrea F., Barrow, Mark P., Rabbani, Naila, Thornalley, Paul J. and O’Connor, Peter B. (2012) Determination of types and binding sites of advanced glycation end products for substance P. Analytical Chemistry, Vol.84 (No.24). pp. 10568-10575. doi:10.1021/ac301583d ISSN 0003-2700.

Research output not available from this repository.

Request-a-Copy directly from author or use local Library Get it For Me service.

Official URL: http://dx.doi.org/10.1021/ac301583d

Request Changes to record.

Abstract

Glycation by endogenous dicarbonyl metabolites such as glyoxal is an important spontaneous post-translational (PTM) modification of peptides and proteins associated with structural and functional impairment. The aim of this study was to investigate types and site of PTM of glyoxal-derived advanced glycation end-products–in the neuropeptide substance P by ultrahigh-resolution Fourier transform ion cyclotron resonance (FTICR), mass spectrometry, and tandem mass spectrometry (MS/MS) experiments. The main site of PTM by glyoxal was the side chain guanidine moiety of the arginine residue. Binding site identification has been achieved by electron capture dissociation, double-resonance electron capture dissociation, and collision-activated dissociation, with assignment of the modified amino acid residue with mass error <1 ppm.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Chemistry
Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Translational & Experimental Medicine > Metabolic and Vascular Health (- until July 2016)
Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Journal or Publication Title: Analytical Chemistry
Publisher: American Chemical Society
ISSN: 0003-2700
Official Date: 2012
Dates:
DateEvent
2012Published
Volume: Vol.84
Number: No.24
Page Range: pp. 10568-10575
DOI: 10.1021/ac301583d
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

Request changes or add full text files to a record

Repository staff actions (login required)

View Item View Item
twitter

Email us: wrap@warwick.ac.uk
Contact Details
About Us