English  |  正體中文  |  简体中文  |  Items with full text/Total items : 26988/38789
Visitors : 2350525      Online Users : 34
RC Version 4.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Adv. Search
LoginUploadHelpAboutAdminister

Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27104

Title: Detection of Proteins and Protein−Ligand Complexes Using HgTe Nanostructure Matrixes in Surface-Assisted Laser Desorption/Ionization Mass Spectrometry
Authors: Cheng-Kang Chiang;Zusing Yang;Yang-Wei Lin;Wen-Tsen Chen;Han-Jia Lin;Huan-Tsung Chang
Contributors: NTOU:Institute of Bioscience and Biotechnology
國立臺灣海洋大學:生物科技研究所
Date: 2010
Issue Date: 2011-10-21T02:22:43Z
Publisher: Analytical Chemistry
Abstract: Abstract:We have analyzed peptides, proteins, and protein−drug complexes through surface-assisted laser desorption/ionization mass spectrometry (SALDI-MS) using HgTe nanostructures as matrixes. We investigated the effects of several parameters, including the concentration of the HgTe nanostructures, the pH of the buffer, and the concentration of salt, on the performance of this system. When HgTe nanostructures are used as matrixes, [M + H]+ ions were the dominant signals. Relative to other commonly used nanomaterials, HgTe nanostructures provided lower background signals from metal clusters, fewer fragment ions, less interference from alkali-adducted analyte ions, and a higher mass range (up to 150 000 Da). The present approach provides limits of detection for angiotensin I and bovine serum albumin of 200 pM and 14 nM, respectively, with great reproducibility (RSD: <25%). We validated the applicability of this method through the detections of (i) the recombinant proteins that were transformed in E. coli, (ii) the specific complex between bovine serum albumin and l-tryptophan, and (iii) a carbonic anhydrase−acetazolamide complex. Our results suggest that this novel and simple SALDI-MS approach using HgTe nanostructures as matrixes might open several new ways for proteomics and the analysis of drug−protein complexes.
Relation: 82(11), pp.4543–4550
URI: http://ntour.ntou.edu.tw/handle/987654321/27104
Appears in Collections:[生命科學暨生物科技學系] 期刊論文

Files in This Item:

File Description SizeFormat
index.html0KbHTML360View/Open


All items in NTOUR are protected by copyright, with all rights reserved.

 


著作權政策宣告: 本網站之內容為國立臺灣海洋大學所收錄之機構典藏,無償提供學術研究與公眾教育等公益性使用,請合理使用本網站之內容,以尊重著作權人之權益。
網站維護: 海大圖資處 圖書系統組
DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback