期刊
JOURNAL OF PROTEOMICS
卷 75, 期 3, 页码 908-913出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.jprot.2011.10.006
关键词
Human whole saliva; Cystatin B; S-glutathionyl; S-cysteinyl; S-S dimer
资金
- Nando Peretti Foundation
- Universita di Cagliari
- Universita Cattolica in Rome
- MIUR
- Italian National Research Council (CNR)
- Regione Sardegna
An HPLC-ESI-MS analysis of adult human whole saliva evidenced three protein masses (M average 11,487 +/- 2, 11,301 +/- 2 and 22,362 +/- 3 Da) eluting in the 32.5-35.0 mwin range. Treatment in reducing conditions allowed establishing that they are S-derivatives of N-terminal acetylated cystatin B, namely its S-glutathionyl, S-cysteinyl and S-S dimer. The identification was confirmed by high resolution HPLC-ESI-MS-MS experiments on the intact naturally occurring proteins and their tryptic digests. S-unmodified cystatin B is rarely detectable in whole saliva of healthy adults (5 subjects out of 65) and its percentage does not overcome approximately 20% of total cystatin B (11 +/- 9%). In the majority of subjects (60 out of 65) the mean percentages of the S-modified derivatives were S-glutathionyl 53 +/- 13%, S-cysteinyl 15 +/- 5%, S-S 2-mer 32 +/- 13%. Variations of the percentages of these S-modified derivatives of cystatin B could be indicative of oral oxidative stress. As we are aware, this is the first time that S-glutathionylation and S-cysteinylation were described as extensive PTM of a salivary protein and the first time that these PTMs were detected in naturally occurring cystatin B. (C) 2011 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据