상세 정보

underline
Metadata Downloads : dc(xml) or Excel
Cited 0 time in scopus ci

Title 

Selective screening of tyrosine-nitrated peptides in tryptic mixtures by in-source photodissociation at 355 nm in matrix-assisted laser desorption ionization

Authors 

Y S ShinJeong Hee MoonM S Kim

Publisher 

American Chemical Society

Issue Date 

2011

Citation 

Analytical Chemistry, vol. 83, no. 5, pp. 1704-1708

Abstract 

Nitration of tyrosine residues in proteins is an important post-translational modification related to various diseases such as Alzheimer's. In this work, efficient and selective photodissociation (PD) at 355 nm was observed for [M + H]+, [M + H - 16]+, and [M + H - 32]+ generated by matrix-assisted ultraviolet laser desorption ionization (UV-MALDI) of tyrosine-nitrated peptides (nitropeptides). Product ion spectra obtained by post-source PD at this wavelength contained useful information on the amino acid sequence. The spectra for nitropeptides obtained with 355 nm irradiation inside the ion source (MALDI/in-source PD) displayed characteristic triplet patterns due to PD of the above ions. For peptides displaying prominent signal in a MALDI mass map of a tryptic mixture, which are mostly those with arginine at the C-terminus, in-source PD allowed positive identification of their tyrosine-nitrated forms. Identification of such nitropeptides was possible at the 10 fmol level (in tryptic digest of 100 fmol BSA).

ISSN 

0003-2700

Link 

http://dx.doi.org/10.1021/ac1028352

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


There are no files associated with this item.
qrcode

FusionCharts.
DSpace Software Coptright(c) 2010 MIT and Hewleft-Packard  /  KRIBB-REPOSITORY ( Email:jakim@kribb.re.kr)