%0 Journal Article
%T Identification of phosphorylation sites of proteins by high performance liquid chromatography-electrospray ionization-quadrupole ion trap mass spectrometry
%A CHE Fayun
%A SHAO Xiaoxia
%A XIA Qichang
%A
中国科学
%J 中国科学C辑(英文版)
%D 2000
%I Springer
%X The phosphorylation sites of two phosphorylated proteins, bovine β-casein and myelin basic protein (MBP), were identified by high performance liquid chromatography-electrospray ionization-quadrupole ion trap mass spectrometry (HPLC-ESI-QITMS). The tryptic digest of each protein was separated by HPLC, the molecular weight of each peptide was determined by ESI-QITMS on line, and MS/MS spectrum of each peptide was simultaneously obtained by the combination of collision-induced desorption (CID) technique and tandem mass spectrometry (MS/MS) of QITMS. The phosphorylated peptide was identified by looking into whether the difference between the observed and predicted molecular weights of a peptide is 80 u or its integral multiple. Then the phosphorylation site was identified through manual interpretation of the MS/MS spectrum of the phosphorylated peptide or automatic SEQUEST data base-searching.
%K high performance liquid chromatography-ion trap mass spectrometry
%K phosphorylation site
%K identification
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=180CF3A72E750F3261A8A60EDC957784&aid=E648DB9DD2A0A854&yid=9806D0D4EAA9BED3&vid=BE33CC7147FEFCA4&iid=B31275AF3241DB2D&sid=B4F9D541F855CF96&eid=6D6B4A516C7DB6EE&journal_id=1674-7305&journal_name=ScienceChina.Lifesciences&referenced_num=0&reference_num=10