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Current developments in SELDI affinity technology
Author(s) -
Tang Ning,
Tornatore Pete,
Weinberger Scot R.
Publication year - 2003
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/mas.10066
Subject(s) - chemistry , affinity chromatography , proteomics , lectin , mass spectrometry , chromatography , computational biology , nanotechnology , biophysics , biochemistry , materials science , biology , gene , enzyme
I. Introduction 34 II. Affinity Probes 35A. Initial Surface‐Affinity Research 36B. Self‐Assembled Monolayers 36C. Dextran 36D. Metal Affinity 36E. Antibody‐ and Protein‐Affinity Probes 37F. Lectin Affinity Capture 38G. Inherent Hydrophobic Interaction Bio‐Probes 38H. Bio‐Molecular Interaction Probes 39 III. SELDI 39A. Fundamentals of SELDI 39B. SELDI in Proteomics 40 IV. Conclusions 41 References 41The overall history and recent advancements in Surface‐Enhanced Laser Desorption/Ionization (SELDI) affinity technology is reviewed. A detailed account of SELDI technology, utilizing Immobilized‐Metal Affinity surfaces, pseudo‐specific chromatographic surfaces, and biospecific interactive surfaces, is presented with particular emphasis placed upon examination of fundamental characteristics as well as specific applications for each. Finally, a detailed review of the specific use of such affinity surfaces in fundamental aspects of clinical, process, and research proteomics activity is presented. © 2003 Wiley Periodicals, Inc., Mass Spec Rev 23:34–44, 2004