Determination of the disulfide bond pattern of a novel C-type lectin from snake venom by mass spectrometry
Article first published online: 29 OCT 2001
Copyright © 2001 John Wiley & Sons, Ltd.
Rapid Communications in Mass Spectrometry
Volume 15, Issue 23, pages 2213–2220, 15 December 2001
How to Cite
Zeng, R., Xu, Q., Shao, X.-X., Wang, K.-Y. and Xia, Q.-C. (2001), Determination of the disulfide bond pattern of a novel C-type lectin from snake venom by mass spectrometry. Rapid Commun. Mass Spectrom., 15: 2213–2220. doi: 10.1002/rcm.500
- Issue published online: 29 OCT 2001
- Article first published online: 29 OCT 2001
- Manuscript Accepted: 23 SEP 2001
- Manuscript Revised: 21 SEP 2001
- Manuscript Received: 23 JUL 2001
- National Natural Science Foundation. Grant Number: 39990600
- National High Technology Project. Grant Number: 102-08-06-02
The disulfide bond pattern of Trimeresurus stejnegeri lectin (TSL), a new member of the C-type lectin family, was determined by mass spectrometry. Four intrachain disulfide bonds of TSL, Cys3-Cys14, Cys31-Cys131, Cys38-Cys133 and Cys106-Cys123, and two interchain linkages, Cys2-Cys2 and Cys86-Cys86, were determined. Three strategies were used in this work. One intrachain (Cys106-Cys123) and one interchain (Cys86-Cys86) disulfide linkages were detected by standard MS methods. The disulfide bonds Cys2-Cys2 and Cys3-Cys14 were analyzed using a modified partial reduction procedure and MS/MS. The last two disulfide bonds were characterized by a MS/MS/MS technique. The strategies developed in this work could be applied more generally to detection of disulfide bond patterns. Copyright © 2001 John Wiley & Sons, Ltd.