骨桥蛋白中多肽片段的FT-ICR-MS分析  

FT-ICR-MS Analysis of the Polypeptide Fragments of Osteopontin

作　　者：石磊[1] 王韶[1] 刘晓梅[1] 程舸[1] 于雷[1] 段芳芳[1] 韩丽华[2] 

机构地区：[1]吉林大学公共卫生学院,吉林长春130021 [2]上海市肿瘤研究所流行病学研究室,上海200032

出　　处：《分析测试学报》2008年第S1期50-52,共3页Journal of Instrumental Analysis

基　　金：吉林省科技厅白求恩医学专项(200705391)

摘　　要：Biological mass spectrometry has received a great progress in recent years.The osteopontin(OPN) isolated and purified from the human milk was studied by HPLC using SCX and C4 columns.After hydrolyzing the purified OPN sample by trypsin,the correlative polypeptide fragments GDSVVYGLR and QNLLAPQTLPSK were obtained by FT-ICR-MS.It showed that the method of nano-spray HPLC combined with FT-ICR-MS and Mascot search was very efficient for the analysis of the purified OPN and its polypeptide fragments.Further study provides more academic theories of their different modifications and the relative bioactivities.Biological mass spectrometry has received a great progress in recent years.The osteopontin(OPN) isolated and purified from the human milk was studied by HPLC using SCX and C4 columns.After hydrolyzing the purified OPN sample by trypsin,the correlative polypeptide fragments GDSVVYGLR and QNLLAPQTLPSK were obtained by FT-ICR-MS.It showed that the method of nano-spray HPLC combined with FT-ICR-MS and Mascot search was very efficient for the analysis of the purified OPN and its polypeptide fragments.Further study provides more academic theories of their different modifications and the relative bioactivities.

关 键 词：osteopontin(OPN) Fourier transform ion CYCLOTRON resonance mass spectrometry(FT-ICR-MS) POLYPEPTIDE FRAGMENTS 

分 类 号：Q51-3[生物学—生物化学]