상세 정보

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

Title 

Observation of phosphorylation site-specific dissociation of singly protonated phosphopeptides

Authors 

Y S ShinJeong Hee MoonM S Kim

Publisher 

Elsevier

Issue Date 

2010

Citation 

Journal of American Society for Mass Spectrometry, vol. 21, no. 1, pp. 53-59

Abstract 

In ultraviolet photodissociation of phosphopeptide ions with a basic residue (arginine, lysine, or histidine) at the N-terminus, intense an - 97 peaks were observed. These ions were formed by cleavage at phosphorylated residues only. For multiply phosphorylated peptides, this site-specific cleavage occurred at every phosphorylated residue. H/D exchange studies showed that an - 97 was formed by H3PO4 loss from an + 1 radical cations. The site-specificity of phosphate loss observed here is in contrast to the nonspecific phosphate loss from bn and yn reported previously. Characteristics of the reaction and its potential utility for phosphopeptide analysis are discussed.

ISSN 

1044-0305

Link 

http://dx.doi.org/10.1016/j.jasms.2009.09.003

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)