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Index Adsorption isotherm, 75, 84 Affinity adsorbent regeneration, 279 Affinity capillary electrophoresis, 303 Affinity column, 112, 123, 151, 226 Affinity displacers, 71, 74, 85 Affinity interactions, characterization of, 98, 103–104 Affinity ligands, 7–9, 11, 14, 39, 93–95, 103, 113, 125, 134, 253, 276 screening of, 103 Affinity macroligands, 43 Affinity of ligands for the target protein, 97 Affinity precipitation, 37–38, 40, 42 hetero-bifunctional format of, 39 Affinity-purified antibodies, 120 Affinity ranking plots, 77 Affinity “tag”, 25 Affinity tags, 13, 192, 212, 229–230 benefits of, 211 AKTA Explorer, 55, 64, 82–83 Amersham Biosciences, 54, 82, 96, 98, 133–134, 217 NHS-activated sepharose, 54 Amicon stirred cell ultrafiltration device, 122 Amines, 96 Aminopeptidases, 184, 229–230 Ammonia aqueous solution, 96 AMP ligands, 6 Amylose affinity chromatography, 169–171, 173, 175–180, 183 Amylose agarose, 182 Amylose biology and chemistry, 172 Amylose matrix, 169, 173–174, 184–186 Anionic heterocyclic substrates, 7 ligand, 320 Antigen-binding peptides, 112 Autofluorescent proteins, 192 Bacillus subtilis, 214 Bacterial cell cultures, 155 lysis, 154–156 Bacterial fermentation, 278 direct lysis of, 155–156 protocol, 281 Bacteriophage, 9–10, 111–112, 123 tips for handling, 123 Bait-Prey binding, 202–203 Balanced salt solution, 250, 252 Basal equilibration buffer, 141, 144 Batch binding, 63–65, 68 chromatography, 63 purification, 159 BCA method, 45, 251, 291, 301 BCA protein assay reagent kit, 98, 288, 291 Bed adsorption plasmid DNA purification, 279 Binding constants, 325 Biological activity-RNase, 267 Biomembrane surfaces, physicochemical properties of, 296 “Biomimetic” affinity adsorbent, 12 Biomolecules, purification of, 1, 72, 125 Biopharmaceutical industry, impact of the, 10 Bioseparation, 37 “Biospecific” affinity techniques, 38 Bis-Substituted-Triazine ligands, 96, 100 Blotto, 115 Canine microsomal membranes, 162 Capillary electrophoresis (CE), 303–304, 315 Catalytic mechanism of cysteine proteases, 222 Cation exchange, 25–27, 74, 85 Cell labeling, 253 lysis reagent, 152–153, 155, 157, 160, 163, 165–166, 277–278 separation, 253 Cellulose-binding domain, 38 Chain-binding protein, 94 Chelating affinity precipitation, 38–40, 42, 47 Chromatographer, 63 Chromatographic column, 72, 248, 250 Chymotrypsin, 4 339
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Affinity Chromatography second edit
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METHODS IN MOLECULAR BIOLOGY TM Aff
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To Tina, Emmanuella, Natalie, and A
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viii Preface Affinity tags for puri
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x Contents 10. Immobilized Metal Io
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xii Contributors Tzong-Hsien Lee
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2 Roque and Lowe cell extract conta
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4 Roque and Lowe groups critical in
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6 Roque and Lowe of reinforcement e
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8 Roque and Lowe unknown factors ar
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10 Roque and Lowe receptor domains
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12 Roque and Lowe A further issue o
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14 Roque and Lowe transgenic system
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16 Roque and Lowe 6. Arsenis, C. an
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18 Roque and Lowe 39. Burton, S.J.,
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20 Roque and Lowe 71. Bhikhabhai, R
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I Various Modes of Affinity Chromat
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26 Charlton and Zachariou Since the
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28 Charlton and Zachariou 5. Equili
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30 Charlton and Zachariou 9. Elute
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32 Charlton and Zachariou 3.3. Puri
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34 Charlton and Zachariou could als
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3 Affinity Precipitation of Protein
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Affinity Precipitation of Proteins
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4 Immunoaffinity Chromatography Stu
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Immunoaffinity Chromatography 55 2.
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Immunoaffinity Chromatography 57 A
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Immunoaffinity Chromatography 59 ab
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5 Dye Ligand Chromatography Stuart
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Dye Ligand Chromatography 63 Develo
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Dye Ligand Chromatography 65 6. Mis
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Dye Ligand Chromatography 67 Fig. 1
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Dye Ligand Chromatography 69 6. Sec
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72 Tugcu chromatography, the sorpti
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74 Tugcu non-specific interactions,
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76 Tugcu the salt counter ions on t
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78 Tugcu On a plot of log K versus
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80 Tugcu Figure 2B illustrates a ty
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82 Tugcu 2.5. Running Displacement
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84 Tugcu then the operating conditi
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86 Tugcu Table 1 Trobleshooting for
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88 Tugcu 23. Torres, A. R. and Pete
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II Affinity Chromatography Using Pu
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94 Roque and Lowe market, with 14 F
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96 Roque and Lowe and RasMol V2.7.1
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98 Roque and Lowe house using, for
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100 Roque and Lowe Gly71 and Gly72)
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102 Roque and Lowe dissolved in ace
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104 Roque and Lowe equilibration bu
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106 Roque and Lowe of color. Purple
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108 Roque and Lowe 5. Fassina, G.,
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8 Phage Display of Peptides in Liga
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Phage Display of Peptides in Ligand
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9 Preparation, Analysis and Use of
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Preparation, Analysis and Use of an
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10 Immobilized Metal Ion Affinity C
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IMAC of Histidine-Tagged Fusion Pro
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152 Godat et al. tag. HQ-tagged pro
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154 Godat et al. 2. NaCl (5 M). 3.
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156 Godat et al. 4. Invert tube to
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158 Godat et al. 3. Sonicate sample
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160 Godat et al. the above protocol
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162 Godat et al. 3.7.1. Purificatio
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164 Godat et al. 3. Adding 200 mM N
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166 Godat et al. 4. The MagneHis Ni
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168 Godat et al. 22. Lin, D., Tabb,
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170 Pattenden and Thomas 1. Introdu
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172 Pattenden and Thomas functions
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174 Pattenden and Thomas of the mal
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176 Pattenden and Thomas necessary.
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178 Pattenden and Thomas 2.4. Amylo
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180 Pattenden and Thomas 9. Thoroug
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182 Pattenden and Thomas 8. Collect
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184 Pattenden and Thomas binding ef
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186 Pattenden and Thomas 15. Cells
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188 Pattenden and Thomas 23. Martin
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13 Methods for Detection of Protein
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Detection of Protein-Protein and Pr
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212 Charlton recognition sequence,
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214 Charlton when selecting Factor
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216 Charlton 2. Materials 2.1. Reag
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218 Charlton (see Notes 12 and 13).
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220 Charlton 3.3. Cleavage of Fusio
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222 Charlton 3. The catalytic mecha
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224 Charlton may dictate. However,
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226 Charlton 22. The full-length fu
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228 Charlton 22. Lien, S., Milner,
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230 Arnau et al. downstream process
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232 Arnau et al. Fig. 1. Overview o
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234 Arnau et al. Fig. 2. The pQE-1
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236 Arnau et al. 2.3.3. Step B Buff
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238 Arnau et al. Fig. 3. Immobilize
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240 Arnau et al. 6. Collect the flo
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242 Arnau et al. 4. Desalting is ne
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III Various Applications of Affinit
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248 Galaev and Mattiasson in biotec
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250 Galaev and Mattiasson 2.4. Sepa
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252 Galaev and Mattiasson 3.4. Sepa
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254 Galaev and Mattiasson ensure el
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17 Monolithic Bioreactors for Macro
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Monolithic Bioreactors for Macromol
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18 Plasmid DNA Purification Via the
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Plasmid DNA Purification 277 are pr
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Plasmid DNA Purification 279 5. Dec
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Plasmid DNA Purification 281 Initia
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Plasmid DNA Purification 283 8. Bou
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286 Tchaga proteins is variable. Ho
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288 Tchaga residue is buried and is
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290 Tchaga 3. Centrifuge the tube a
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292 Tchaga 5. Use the BCA Protein A
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294 Tchaga 24. Figeys D., Gygi S.P.
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296 Lee and Aguilar The primary dif
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298 Lee and Aguilar 2.2. Equipment
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300 Lee and Aguilar Abs 280 PLA 2 A
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302 Lee and Aguilar 9. Pidgeon, C.,
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304 Heegaard et al. 1. Introduction
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Table 1 CE Methods and Their Corres
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308 Heegaard et al. Fig. 1. Images
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310 Heegaard et al. characteristics
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312 Heegaard et al. sample. A final
Page 622: 314 Heegaard et al. Especially usef
Page 626: 316 Heegaard et al. parameters extr
Page 630: 318 Heegaard et al. f M s 5.0 0.01
Page 634: 320 Heegaard et al. where AL is the
Page 638: 322 Heegaard et al. Fig. 6. Mobilit
Page 642: 324 Heegaard et al. Fig. 7. Drug-pr
Page 646: 326 Heegaard et al. 6.2.1.3. Equati
Page 650: 328 Heegaard et al. 2. Introduce pr
Page 654: 330 Heegaard et al. 9. The sample s
Page 658: 332 Heegaard et al. 21. Grossman, P
Page 662: 334 Heegaard et al. 52. Kautz, R. A
Page 666: 336 Heegaard et al. 82. Berezovski,
Page 670: 338 Heegaard et al. 111. Heegaard,
Page 676: Index 341 Genenase I, 170, 214, 215
Page 680: Index 343 Saccharomyces cerevisae,
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