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Blotting–Electroblotting 319 ued for too long. <strong>Protein</strong>s migrate faster from SDS gels (they are coated with SDS and highly charged), and transfer from non-SDS gels takes longer (around 4–5 h). 7. Other proteins can be used for blocking (e.g., albumin, hemoglobin), but dried milk powder is usually the best option. Thirty-minute incubation with blocking protein is sufficient to saturate all the protein binding sites on the blot. Longer times and overnight incubation can be used if this is more convenient. <strong>Protein</strong> blocked sheets can be stored frozen for long periods. For this, drain excess blocking solution and place in a plastic bag when required, wash with blocking buffer for 10 min, then continue with the next processing steps. References 1. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350–4354. 2. Johnstone, A. and Thorpe, R. (1996) Immunochemistry in Practice, 3rd ed. Blackwell Scientific, Oxford, UK.
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The Protein Protocols Handbook SECO
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The Protein Protocols Handbook SECO
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Preface The Protein Protocols Handb
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viii Contents 14 Identification of
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x Contents 47 Conjugation of Fluoro
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xii Contents 80 Peptide Mapping by
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xiv Contents 112 Sialic Acid Analys
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xvi Contents 145 Purification of Ig
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Contributors THOMAS E. ADRIAN • D
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Contributors xxi RUTH R. FRENCH •
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Contributors xxiii STEFANIE A. NELS
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UV Absorption 1 PART I QUANTITATION
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4 Aitken and Learmonth 2. Materials
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6 Aitken and Learmonth References 1
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8 Waterborg 3. Method 1. To 0.1 mL
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BCA for Protein Quantitation 11 3 T
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BCA for Protein Quantitation 13 Tab
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The Bradford Method 15 4 The Bradfo
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The Bradford Method 17 Fig. 1. Vari
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The Bradford Method 19 Table 2 Comp
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The Bradford Method 21 13. Kirazov,
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24 Akins and Tuan passes. The side
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26 Akins and Tuan Fig. 2. Effect of
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28 Akins and Tuan protein concentra
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30 Akins and Tuan energy. Too much
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32 Boerner et al. Several approache
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34 Boerner et al. Fig. 2. 3-Nitroty
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36 Boerner et al. containing Tris,
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38 Boerner et al. 2.2. Nitric Acid
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40 Boerner et al. 8. Böhlen, P., S
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42 Aitken and Learmonth 1.2. Measur
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44 Aitken and Learmonth References
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46 Friedrich et al. 2. Materials 2.
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48 Friedrich et al. Fig. 1. Differe
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50 Friedrich et al. References 1. S
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52 Root and Wang Fig. 1. Representa
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54 Root and Wang 4. Kinetic silver
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Gel Electrophoresis of Proteins 57
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Gel Electrophoresis of Proteins 59
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SDS-PAGE 61 11 SDS Polyacrylamide G
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SDS-PAGE 63 their own rates. A more
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SDS-PAGE 65 7. To ensure that the g
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SDS-PAGE 67 close to the dye, and t
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70 Walker 2. Buffers: a. 1.875 M Tr
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72 Walker Fig. 2. Diagrammatic repr
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74 Judd 2. Materials 2.1. Equipment
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76 Judd ber with anode buffer. Remo
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78 Judd 4. Run the gel as described
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SDecS-PAGE of Nucleic Acid Binding
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CAT Gel Electrophoresis 87 15 Cetyl
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CAT Gel Electrophoresis 89 Fig. 1.
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CAT Gel Electrophoresis 91 3. CAT s
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CAT Gel Electrophoresis 93 Table 1
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CAT Gel Electrophoresis 95 the tank
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CAT Gel Electrophoresis 97 may be a
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CAT Gel Electrophoresis 99 enzyme p
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CAT Gel Electrophoresis 101 20. Rey
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104 Waterborg Fig. 1. Histones of t
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106 Waterborg 9. Riboflavin-5'-phos
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108 Waterborg 25. Remove the bottom
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110 Waterborg 10. The amount of pro
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AUT Gel for Histones 113 17 Acid-Ur
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AUT Gel for Histones 115 Details of
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AUT Gel for Histones 117 Fig. 2. (A
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AUT Gel for Histones 119 13. Add 0.
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AUT Gel for Histones 121 5. The sep
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AUT Gel for Histones 123 15. Waterb
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126 Walker the cost of preparing IE
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128 Walker 4. Notes 1. The sucrose
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Protein Solubility in 2-D Electroph
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Fractionated Extraction 141 20 Prep
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Fractionated Extraction 143 Fig. 1.
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Fractionated Extraction 145 Table 2
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Fractionated Extraction 147 13. Com
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149 SI + II fraction: liver Brain H
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Fractionated Extraction 151 3. Add
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Fractionated Extraction 153 Fig. 2.
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Fractionated Extraction 155 and bra
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Fractionated Extraction 157 ume are
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160 Bizios 2. Materials 2.1. Equipm
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162 Bizios 5. Sample preparation sh
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164 Gravel Fig. 1. Tube Cell Model
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166 Gravel 3. Fill the lower chambe
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168 Gravel lysis solution A (SDS-DT
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170 Gianazza Fig. 1. Structure of t
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172 Gianazza Table 1 pK Values of I
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174 Gianazza Fig. 2. Course of the
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176 Gianazza Table 3 IPG 4-7 and 6-
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178 Gianazza the gel. Depending on
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180 Gianazza 17. Chiari, M., Pagani
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182 Lopez 3. Slide a grommet onto e
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DIGE 185 25 Difference Gel Electrop
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DIGE 187 2.2. IEF Fig 1. The two cy
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DIGE 189 3. Method 3.1. Sample Solu
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DIGE 191 Strips, the instructions t
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DIGE 193 2. Push the strip down unt
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DIGE 195 4. The presence of Pharmal
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Comparing 2-D Gels on the Internet
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Immunoblotting of 2-DE Separated Pr
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232 Springer Fig. 1. Comparison of
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234 Springer Table 1 Recipe for Var
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Quantification of Proteins on Gels
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Rapid Staining with Nile Red 243 30
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Rapid Staining with Nile Red 245 Fi
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Rapid Staining with Nile Red 247 11
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Rapid Staining with Nile Red 249 Re
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252 Fernandez-Patron to years witho
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254 Fernandez-Patron Fig. 2. Revers
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256 Fernandez-Patron spectrometry (
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258 Fernandez-Patron 11. Fernandez-
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260 Choi, Hong, and Yoo Table 1 Lin
Page 269 and 270: 262 Choi, Hong, and Yoo Fig. 2. Mec
Page 271 and 272: Silver Staining of Proteins 265 33
Page 273 and 274: Silver Staining of Proteins 267 Fig
Page 275 and 276: Silver Staining of Proteins 269 3.3
Page 277 and 278: Silver Staining of Proteins 271 12.
Page 279 and 280: 274 Patton plexes for colorimetric
Page 281 and 282: 276 Patton device (CCD) camera. The
Page 283 and 284: 278 Patton 3.2. Luminescent Detecti
Page 285 and 286: 280 Patton 3.5. Luminescent Detecti
Page 287 and 288: 282 Patton EDTA, pH 9.6 or using SY
Page 289 and 290: 284 Patton filter. Proteins stained
Page 291 and 292: 286 Patton 17. Lim, M., Patton, W.,
Page 293 and 294: 288 Dunn variations in silver stain
Page 295 and 296: 290 Dunn Fig. 1. A 2-DE separation
Page 297 and 298: 292 Dunn 11. Stephens, R. E. (1975)
Page 299 and 300: Gels Using Eosin Y Stain 295 36 Det
Page 301 and 302: Gels Using Eosin Y Stain 297 3. An
Page 303 and 304: 300 Jenö and Horst and Coomassie B
Page 305 and 306: 302 Jenö and Horst Fig. 1. Side (A
Page 307 and 308: 304 Jenö and Horst BT1 membrane, o
Page 309 and 310: Autoradiography and Fluorography 30
Page 317 and 318: Blotting-Electroblotting 315 PART I
Page 319: 318 Page and Thorpe 4. Filter paper
Page 323 and 324: 322 Gravel Fig. 1. Plasma proteins
Page 325 and 326: Table 1 Examples of Transfer Buffer
Page 327 and 328: Table 1 (continued) Exampled of Tra
Page 329 and 330: 328 Table 2 (continued) Membranes U
Page 331 and 332: 330 Gravel Table 3 Blocking Agents
Page 333 and 334: 332 Gravel PVDF membranes are more
Page 335 and 336: 334 Gravel 15. Jin, Y. and Cerletti
Page 337 and 338: 336 Walker 3. Whatman 3MM filter pa
Page 339 and 340: 338 Delcuve and Davie of Tris base
Page 341 and 342: 340 Delcuve and Davie 3. The transf
Page 343 and 344: Alkaline Phosphates Labeling of IgG
Page 345 and 346: β-Galactosidase Labeling of IgG An
Page 347 and 348: HRP Labeling of IgG Antibody 347 45
Page 349 and 350: Digoxigenin Labeling of 1gG Antibod
Page 351 and 352: Conjugation of Fluorochromes 351 47
Page 353 and 354: Conjugation of Fluorochromes 353 7.
Page 355 and 356: Coupling of Abs with Biotin 355 48
Page 357 and 358: Coupling of Abs with Biotin 357 Fig
Page 359 and 360: Coupling of Abs with Biotin 359 3.
Page 361 and 362: Coupling of Abs with Biotin 361 Fig
Page 363 and 364: Coupling of Abs with Biotin 363 12.
Page 365 and 366: 366 Haugland and Bhalgat sidered, i
Page 367 and 368: 368 Haugland and Bhalgat (23), with
Page 369 and 370: 370 Haugland and Bhalgat 1. Wash si
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372 Haugland and Bhalgat adding 1/1
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374 Haugland and Bhalgat 19. Dean,
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376 Alba and Daban Fig. 1. Accordin
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378 Alba and Daban 9. Mark with a s
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Copper Iodide Staining of Proteins
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Page 385 and 386:
388 Hong et al. 2. Materials 2.1. G
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390 Hong et al. Table 1 Comparison
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392 Hong et al. References 1. Towbi
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394 Fowler Fig. 1. Principle of the
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396 Fowler There are two approaches
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398 Fowler Fig. 4. Detection of bou
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400 Fowler Table 1 Troubleshooting
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402 Fowler Table 3 Troubleshooting
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404 Fowler 18. Schapira, A. H. V. (
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406 Kruger Table 1 Variation in Spe
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408 Kruger 7. Horseradish peroxidas
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410 Kruger Brilliant Blue is unsuit
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412 Kruger equally effective. The s
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414 Kruger References 1. Blake, M.
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416 Santora et al. Fig. 1. Diagramm
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418 Santora et al. 7. After allowin
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Chemifluorescence 421 56 Detection
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Chemifluorescence 423 1. Like chemi
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Chemifluorescence 425 11. Excess re
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Chemifluorescence 427 Fig. 1. β-Ga
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Western Blotting Using ECL 429 57 Q
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Western Blotting Using ECL 431 In t
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Western Blotting Using ECL 433 Fig.
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Western Blotting Using ECL 435 Tabl
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Western Blotting Using ECL 437 4. F
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440 Kaufmann particular antigen are
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442 Kaufmann Fig.1. Reutilization o
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444 Kaufmann (Amersham Pharmacia Bi
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446 Kaufmann 2. Rather than exposin
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448 Kaufmann Fig. 3. Conditions for
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450 Kaufmann erasure buffer (16). I
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452 Kaufmann 10. Laycock, C. A., Ph
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Carboxymethylation of Cysteine 455
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Performic Acid Oxidation 457 60 Per
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Succinylation of Proteins 459 61 Su
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Pyridylethylation 461 62 Pyridyleth
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Fig. 2. The MALDI mass spectrum of
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466 Tawfik reagent. Dramatic pK a c
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Nitration of Tyrosines 469 64 Nitra
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Nitration of Tyrosines 471 1. Nitra
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Ethoxyformylation of Histidine 65 E
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p-Hydroxyphenylglyoxal-Modified Arg
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Amidation of Carboxyl Groups 477 67
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Amidination of Lysine 479 68 Amidin
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Modification of Trytophan 481 69 Mo
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Modification of Sulfhydryl Groups 7
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Cleavage at Methionyl-X Bonds 485 7
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Cleavage at Methionyl-X Bonds 487 F
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Cleavage at Methionyl-X Bonds 489 c
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Cleavage at Methionyl-X Bonds 491 1
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Table 1 Summary of Methods for Clea
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496 Smith 2. Materials 1. Oxidizing
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498 Smith References 1. Kilic, F. a
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500 Smith Fig. 1 Mechanisms of the
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502 Smith 5. Schulz, A., Marx, U. C
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504 Smith 3. NaOH solution, suffici
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506 Smith 7. Tu, B. P. and Wang, J.
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508 Smith Fig. 1. Illustration of r
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510 Smith ine-ADP-ribose bonds (in
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512 Stone and Williams 3. Sequencin
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514 Stone and Williams analysis ind
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516 Stone and Williams 9. If the ge
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518 Stone and Williams disadvantage
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520 Table 1 Summary of 88 In-Gel Di
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Enzymatic Digestion of Membrane-Bou
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Reverse-Phase HPLC Separation 533 7
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Reverse-Phase HPLC Separation 535 3
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Reverse-Phase HPLC Separation 537 F
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Reverse-Phase HPLC Separation 539 m
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2-D TLE-TLC Mapping 541 PART V PROT
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544 Judd 2. Power pack (e.g., EC 42
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546 Judd 4. Excise the protein band
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548 Judd easy to use and reliable,
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550 Judd 4. Use a graduated, 1-5 µ
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552 Judd 2. Laemmli, U. K. (1970) C
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554 Judd 2.2. Electroblotting (for
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556 Judd 3.2.2.2. PROTEIN IN-GEL SL
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HPLC Mapping 559 81 Peptide Mapping
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HPLC Mapping 561 should yield adequ
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564 Walker and Sweeney leucine amin
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566 Walker and Sweeney 4. Narahashi
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568 Kochhar et al. Fig.1. Marfey’
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570 Kochhar et al. Table 1 HPLC Pro
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572 Kochhar et al. 12. Wu, G. and F
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574 Irvine As well as being a stand
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576 Irvine Fig. 1. Separation of a
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578 Irvine K d can be calculated fr
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Disulfide-Linked Peptide Detection
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Disulfide-Linked Peptide Detection
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586 Aitken and Learmonth Selective
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588 Aitken and Learmonth Acknowledg
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590 Aitken and Learmonth 3. Whatman
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592 Aitken and Learmonth Fig. 1. Di
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Ellman’s Reagent 595 88 Estimatio
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Cysteine Residues and Disulfide Bon
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Analyzing Protein Phosphorylation 6
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Mass Spectrometry of Protein Phosph
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Carboxyl Methyltransferase 623 92 I
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Carboxyl Methyltransferase 625 5. S
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Carboxyl Methyltransferase 627 3.4.
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Carboxyl Methyltransferase 629 Fig.
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Carboxyl Methyltransferase 631 6. G
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634 Grassie and Milligan group to t
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636 Grassie and Milligan 3.3. Immun
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638 Grassie and Milligan 6. When pr
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Radiolabeled Prenyl Alcohols and An
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Analysis of Isoprenylated Proteins
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674 Dowdy 5. Speed Vac or lyophiliz
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676 Dowdy 3.3. Trypsinization of Pr
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678 Dowdy Fig. 2. A cross-sectional
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680 Dowdy 5. Hardie, D. G. (1993) P
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682 Wada 2. Detection of variants t
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684 Wada Fig. 1. Detection of a var
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686 Wada Fig. 3. ESI mass spectrum
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688 Wada Fig. 5. FAB mass spectra o
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690 Wada Fig. 9. FAB mass spectra o
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692 Wada 4. Protein variants are he
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694 Jensen and Wilm Fig. 1. Nanoele
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696 Jensen and Wilm 10, 200; 2-490,
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698 Jensen and Wilm Be aware that t
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700 Jensen and Wilm the same as use
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702 Jensen and Wilm Fig. 4. Parent
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704 Jensen and Wilm Fig.6. Peptide
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706 Jensen and Wilm b 2 and a 2 fra
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708 Jensen and Wilm Another method
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710 Jensen and Wilm 28. Yates, J. R
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712 Courchesne and Patterson Fig. 1
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714 Courchesne and Patterson 2.7. M
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716 Courchesne and Patterson for 3
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718 Courchesne and Patterson 2. The
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720 Courchesne and Patterson with t
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722 Courchesne and Patterson 3.5.2.
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724 Courchesne and Patterson Table
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726 Courchesne and Patterson the im
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728 Courchesne and Patterson it is
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730 Courchesne and Patterson 31. Mo
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732 Courchesne and Patterson 30. Bi
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734 Wang and Chait Fig. 1. The prin
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736 Wang and Chait 8. Mass spectrom
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738 Wang and Chait Fig. 2. Amino ac
Page 722 and 723:
Sequence Analysis with WinGene/WinP
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Page 728 and 729:
Proteins Cross-linked to DNA by Cis
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Page 734 and 735:
754 Spencer and Davie 2. Hepes buff
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756 Spencer and Davie Fig. 1. Sodiu
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Glycoprotein Detection 759 PART VI
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762 Packer et al. in sugars of glyc
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764 Packer et al. c. Solution 3: 75
Page 744 and 745:
766 Packer et al. 2. Incubate the m
Page 746 and 747:
768 Packer et al. product, Pro-Q Em
Page 748 and 749:
770 Packer et al. 9. The postlabeli
Page 750 and 751:
772 Packer et al. 24. The HPLC syst
Page 752 and 753:
774 Møller and Poulsen are stained
Page 754 and 755:
776 Møller and Poulsen gel can be
Page 756 and 757:
Lectin Blotting to Detect Glycoprot
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Page 764 and 765:
787 Lens culinaris Man GlcNAc(β-1,
Page 766 and 767:
789 Sambucus nigra NeuAc NeuAc(α-2
Page 768 and 769:
Page 770 and 771:
Page 772 and 773:
Lectin-Binding Assay for Glycoanaly
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Page 776 and 777:
Page 778 and 779:
Page 780 and 781:
Chemical Methods of Analysis 803 10
Page 782 and 783:
HPAEC 805 109 Monosaccharide Analys
Page 784 and 785:
HPAEC 807 2. Townsend, R. R. (1995)
Page 786 and 787:
810 Hounsell, Davies, and Smith 9.
Page 788 and 789:
812 Hounsell, Davies, and Smith 3.
Page 790 and 791:
Sialic Acid Analysis by HPAEC-PAD 8
Page 792 and 793:
Oligosaccharide Chains 817 113 Chem
Page 794 and 795:
Short Chapter Title 819 114 O-Linke
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O-Linked Oligosaccharide Profiling
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Release of N-Linked Oligosaccharide
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Release of N-Linked Oligosaccharide
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Enzymatic Release 827 117 Enzymatic
Page 804 and 805:
PGC 829 118 N-Linked Oligosaccharid
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N-Linked Oligosaccharide Profiling
Page 808 and 809:
Oligosaccharide Substrates for Exog
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Page 812 and 813:
Page 814 and 815:
Page 816 and 817:
842 Wong et al. teins. The base is
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844 Wong et al. 3.4. Modification a
Page 820 and 821:
846 Wong et al. Table 1 Theoretical
Page 822 and 823:
Table 3 Binding Preferences of Digo
Page 824 and 825:
850 Wong et al. 6. Lauritzen, E., M
Page 826 and 827:
852 Brandley, Klock, and Starr unsu
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854 Brandley, Klock, and Starr N-li
Page 830 and 831:
856 Brandley, Klock, and Starr 6. A
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858 Brandley, Klock, and Starr Fig.
Page 834 and 835:
860 Brandley, Klock, and Starr achi
Page 836 and 837:
862 Brandley, Klock, and Starr 7. H
Page 838 and 839:
HPLC of Fluorescently Labeled Glyca
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Page 858 and 859:
886 Fotinopoulou and Turner Fig. 1.
Page 860 and 861:
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Page 864 and 865:
Sequencing Heparan Sulfate Sacchari
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Page 872 and 873:
Page 874 and 875:
Page 876 and 877:
Monitoring Glycoprotein Heterogenei
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Page 888 and 889:
918 Yamamoto, Tsuji, and Osawa Fig.
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920 Yamamoto, Tsuji, and Osawa 2. D
Page 892 and 893:
922 Yamamoto, Tsuji, and Osawa Fig.
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924 Yamamoto, Tsuji, and Osawa 3.4.
Page 896 and 897:
926 Yamamoto, Tsuji, and Osawa 3.7.
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928 Yamamoto, Tsuji, and Osawa 4. C
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930 Yamamoto, Tsuji, and Osawa 16.
Page 902 and 903:
Antibody Production 933 PART VII AN
Page 904 and 905:
936 Burns as a primary one and moun
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938 Burns The legislation in terms
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940 Burns will not elicit an immune
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942 Amero, James, and Elgin 11. Spa
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944 Amero, James, and Elgin ously i
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946 Diano and Le Bivic Because conv
Page 916 and 917:
948 Diano and Le Bivic Fig. 1. Exci
Page 918 and 919:
950 Diano and Le Bivic Fig. 3. Seco
Page 920 and 921:
952 Diano and Le Bivic tual excess
Page 922 and 923:
954 Adrian 2.2. Protein Carriers Fa
Page 924 and 925:
Table 1 Bifunctional Cross-linking
Page 926 and 927:
958 Adrian lation and may serve to
Page 928 and 929:
960 Adrian confirming that it is im
Page 930 and 931:
The Chloramine T Method 963 132 The
Page 932 and 933:
The Chloramine T Method 965 Referen
Page 934 and 935:
968 Bailey 4. Notes 1. The exact na
Page 936 and 937:
970 Bailey 4. Notes 1. [ 125 I] Bol
Page 938 and 939:
972 Conlon Fig. 1. The structure of
Page 940 and 941:
974 Conlon Fig. 2. RP-HPLC on a (0.
Page 942 and 943:
976 Conlon 8. The relatively steep
Page 944 and 945:
Purification and Assessment of Qual
Page 946 and 947:
Purification and Assessment of Qual
Page 948 and 949:
Precipitation of IgG 983 137 Purifi
Page 950 and 951:
Isolation of IgG 985 138 Purificati
Page 952 and 953:
988 Page and Thorpe 2. Apply the sa
Page 954 and 955:
990 Dolman, Page, and Thorpe 4. Loa
Page 956 and 957:
Protein A or Protein G 993 142 Puri
Page 958 and 959:
Purification of IgG Using SE-HPLC 9
Page 960 and 961:
Purification of IgG Using SE-HPLC 9
Page 962 and 963:
1000 Page and Thorpe 9. IgG prepara
Page 964 and 965:
Short Chapter Title 1003 145 Purifi
Page 966 and 967:
Electrophoresis 1005 146 Analysis o
Page 968 and 969:
Electrophoresis 1007 2. The extinct
Page 970 and 971:
1010 Bird and Thorpe 4. Centrifuge.
Page 972 and 973:
Synthetic Ligands for Ig Purificati
Page 974 and 975:
Page 976 and 977:
Page 978 and 979:
Page 980 and 981:
Page 982 and 983:
Page 984 and 985:
Western Cross-Blotting 1025 149 Det
Page 986 and 987:
Western Cross-Blotting 1027 2.3. Cr
Page 988 and 989:
Western Cross-Blotting 1029 3.2. El
Page 990 and 991:
Western Cross-Blotting 1031 Fig. 2.
Page 992 and 993:
Western Cross-Blotting 1033 tor she
Page 994 and 995:
1036 Kipriyanov Fig. 1. Schematic r
Page 996 and 997:
1038 Kipriyanov 9. 1× Tris-acetate
Page 998 and 999:
1040 Kipriyanov 2. Run 15-20 polyme
Page 1000 and 1001:
1042 Kipriyanov 9. For analytical s
Page 1002 and 1003:
1044 Kipriyanov nant antibodies sta
Page 1004 and 1005:
1046 Kipriyanov 35. Laemmli, U. K.
Page 1006 and 1007:
1048 Andrew Fig. 1. Diagramatic rep
Page 1008 and 1009:
1050 Andrew 3.3. Preparation of Fab
Page 1010 and 1011:
1052 Andrew 3. Parham, P. (1983) On
Page 1012 and 1013:
1054 French Fig. 1. Preparation of
Page 1014 and 1015:
1056 French 1. Use equal amounts of
Page 1016 and 1017:
1058 French region disulfide bonds.
Page 1018 and 1019:
1060 Ehrlich, Berthold, and Bailon
Page 1020 and 1021:
Page 1022 and 1023:
Page 1024 and 1025:
Page 1026 and 1027:
Page 1028 and 1029:
Page 1030 and 1031:
Page 1032 and 1033:
1074 Dörsam et al. with the phagem
Page 1034 and 1035:
1076 Dörsam et al. 29. 100 mM Trie
Page 1036 and 1037:
1078 Dörsam et al. 5. Centrifuge t
Page 1038 and 1039:
1080 Dörsam et al. 15. A negative
Page 1040 and 1041:
1082 Dörsam et al. 17. Larrick, J.
Page 1042 and 1043:
1084 Jordan Fig. 1. The indirect sa
Page 1044 and 1045:
1086 Jordan 11. Streptavidin HRP (s
Page 1046 and 1047:
1088 Jordan a suitable plate is by
Page 1048 and 1049:
1090 Stott Fig 1. Chemiluminescent
Page 1050 and 1051:
1092 Stott Fig. 2. Origin of light
Page 1052 and 1053:
1094 Stott 3. For best possible sen
Page 1054 and 1055:
1096 Stott 10. Stanley, P. E. (1992
Page 1056 and 1057:
1098 Johansen and Svensson Table 1
Page 1058 and 1059:
Page 1060 and 1061:
Page 1062 and 1063:
1104 Johansen and Svensson 4. If th
Page 1064 and 1065:
1106 Johansen and Svensson 12. Take
Page 1066 and 1067:
Short Chapter Title 1109 158 Immuno
Page 1068 and 1069:
Hybridoma Production 1111 159 Hybri
Page 1070 and 1071:
Hybridoma Production 1113 15. After
Page 1072 and 1073:
1116 Page and Thorpe 3. Wash the pl
Page 1074 and 1075:
1118 Page and Thorpe 3. Wash the pl
Page 1076 and 1077:
1120 Page and Thorpe medium by incr
Page 1078 and 1079:
1122 Schwarz Table 1 Affinity of Pr
Page 1080 and 1081:
1124 Schwarz 2.2. General Purificat
Page 1082 and 1083:
1126 Schwarz 3.5. General Purificat
Page 1084 and 1085:
1128 Schwarz 7. Schulze, R. A., Kon
Page 1086 and 1087:
1130 Thi Man and Morris Table 1 Exa
Page 1088 and 1089:
1132 Thi Man and Morris 10. 1000X A
Page 1090 and 1091:
1134 Thi Man and Morris 300g. Resus
Page 1092 and 1093:
1136 Thi Man and Morris 3.8. Antibo
Page 1094 and 1095:
1138 Thi Man and Morris Further Rea
Page 1096 and 1097:
1140 Index Auroprobe BL plus, 397-3
Page 1098 and 1099:
1142 Index detection of disulfide l
Page 1100 and 1101:
1144 Index Phenol-sulfuric acid ass
Page 1102 and 1103:
1146 Index W Western blotting (see
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