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|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|
|Citation:||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|
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