Abstract
| I. | Introduction | 34 |
| II. | Affinity Probes | 35 |
| | A. Initial Surface‐Affinity Research | 36 |
| | B. Self‐Assembled Monolayers | 36 |
| | C. Dextran | 36 |
| | D. Metal Affinity | 36 |
| | E. Antibody‐ and Protein‐Affinity Probes | 37 |
| | F. Lectin Affinity Capture | 38 |
| | G. Inherent Hydrophobic Interaction Bio‐Probes | 38 |
| | H. Bio‐Molecular Interaction Probes | 39 |
| III. | SELDI | 39 |
| | A. Fundamentals of SELDI | 39 |
| | B. SELDI in Proteomics | 40 |
| IV. | Conclusions | 41 |
| References | 41 |
The 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