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340 Index Cibacron blue, 6–7, 61 Clarified lysate, 129, 134 Cloning vectors, 154, 196, 234 Clontech’s phospho-specific metal ion affinity, 288 Column chromatography, 4, 63 enrichment, 290 equilibration, 299 fractions, 68 regeneration, 301 Combinatorial ligand synthesis, 8 Convective interaction media, 257–259, 272 Copolymers of vinylimidazole, 40 Coupling, 54–56, 58, 106, 115, 249–251 affinity ligand, 249, 251 Covalent attachment of proteins, 206 Crotalus artox venom powder, 298 Cryogels, 247, 248 Cyanogen bromide, 4 Cyanuric chloride activation, 100 recrystallization, 106 Cysteine protease, inhibitors of, 226 Cytoplasmic expression, 170, 172, 185 DAPase test for pyroglutamyl removal, 236, 240 De Novo ligand design, 7 Designed ligands, 93 Dialysis cassettes, 54, 63 of the protein, 67 Displacement chromatogram, 83 Displacement chromatography, 71–75, 77, 82 critical components of, 71, 73 trobleshooting for, 86 Displacement zone, 73, 85 Displacer affinity, 71, 73, 79 ranking plots, 79 Displacer concentration, 77–78, 80–81, 85 DNA sequencing, 118, 277 DNase immobilization, 262 Downstream processing, 10, 94, 125, 230 Drug-plasma protein solutions, 330 Dual affinity protein, 275 Dulbecco’s Modified Eagle’s Medium, 204 Dye affinity chromatography, development of a, 63 Dye ligand chromatography, 61–62, 64, 66 resins, 63 Dynamic affinity, 77 Dynamic immobilization method, 260 E. coli, 9, 13, 115, 118, 129, 134, 140, 170–173, 192, 220, 231, 233–235, 237–238, 248–249, 280, 295 Efficiency of, 269 Elastin-like proteins, 42 Electroendosmotic (EEO) flow, 307–308 Electrophoresis buffer, 303, 305, 309–311, 313–315, 317–318, 320–321, 323, 325–327, 329–330 Electrospray ionization (ESI), 314 ELISA tests, 15, 53, 98, 104–105, 107, 115–119, 121–123, 253 isotype control, 119 rounds of panning by, 116 Elution buffer, 28, 48 , 55–56, 62–65, 97, 104, 113, 115–116, 120, 127, 133–135, 141, 143, 146, 148, 152, 158–160, 162–165, 175–181, 183, 195–196, 201, 203, 249–250, 277, 279, 291, 295 Elution chromatography, 71, 73, 75, 80 Elution fractions, 133, 135, 276–277, 279, 281 Elution from Magnetic Particles, 165 Enterokinase, 170, 213, 217, 222, 225 Enzyme activation, 242 commission number, 5 immobilization, 196, 206 –ligand interactions, 5 reactor, 262, 264, 267, 271, 273 use of, 271 Epichlorohydrin, 96 Epoxy activated adsorbent, 128 agarose beads, 105 Eppendorf tubes, 98, 104, 200, 202 Expanded bed adsorption, 94, 126, 130, 279 ExPASy ProtParam tool, 133, 184 Fast protein liquid chromatography (FPLC), 169–170, 178, 181 FastBreak Cell Lysis Reagent, 152–153, 155, 160, 163, 165–166 Fermentation, 126, 129, 247–249, 252, 275, 278, 280–281 Flow cytometer, 254 Fluorescein isothiocyanate based screening, 97 Fluorescence polarization analysis, 192 ‘foldable’ protein, 171 Food and Drug Administration (FDA), 12, 93–94 approved monoclonal antibodies, 94 Fusion protein cleavage, 212, 215 reagents for, 216
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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
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Page 642: 324 Heegaard et al. Fig. 7. Drug-pr
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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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