Please use this identifier to cite or link to this item:
|Title:||Purpureotin: A novel di-dimeric C-type lectin-like protein from Trimeresurus purpureomaculatus venom is stabilized by noncovalent interactions|
|Keywords:||C-type lectin-like protein|
|Source:||Li, X., Zheng, L., Kong, C., Kolatkar, P.R., Chung, M.C.M. (2004-04-01). Purpureotin: A novel di-dimeric C-type lectin-like protein from Trimeresurus purpureomaculatus venom is stabilized by noncovalent interactions. Archives of Biochemistry and Biophysics 424 (1) : 53-62. ScholarBank@NUS Repository. https://doi.org/10.1016/j.abb.2004.01.015|
|Abstract:||Purpureotin, a novel di-dimeric C-type lectin-like protein (CLP) from Trimeresurus purpureomaculatus, was purified and sequenced. While its native molecular mass was determined to be 63kDa, purpureotin showed a single band of 30kDa on nonreducing SDS-PAGE and two polypeptide chains (16.0 and 14.5kDa) under reducing condition. These results were subsequently confirmed by mass spectrometric analyses. Based on these results, we postulate that purpureotin is a dimer of the α,β-heterodimer which is held together by noncovalent interactions. Molecular modeling studies indicate that a dimer of α,β-heterodimers can be formed where the α chains are held together by electrostatic charges and β chains via hydrophobic interactions. Functionally, purpureotin induced platelet aggregation without any cofactor in a dose-dependent manner. However, the platelet aggregation effect was blocked by echicetin. Therefore, purpureotin is assumed to be a GPIb-binding protein which binds to the same or a closely related GPIb site on platelets as echicetin. © 2004 Elsevier Inc. All rights reserved.|
|Source Title:||Archives of Biochemistry and Biophysics|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Feb 15, 2018
WEB OF SCIENCETM
checked on Jan 30, 2018
checked on Feb 19, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.