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787 Lens culinaris Man GlcNAc(β-1,2)Man(α-1,6) Fuc(α-1,6) (LCA) Man(β-1,4)GlcNAc(β-1,4)GlcNAc(β-1,N)Asn GlcNAc(β-1,2)Man(α-1,3) Note: LCA is specific of mannose (α-1,3) or (α-1,6). Fucose (α-1,6) linked to GlcNAc is required for the reaction (3). Galanthus nivalis Terminal Man(α-1,2)(α-1,3) or (α-1,6)Man (GNA) Man Note: GNA is particularly useful for identifying high mannose or hybrid type oligosaccharide structure because it does not react (unlike ConA) with biantennary complex type chains (21,22). Datura GlcNAc [Gal(β-1,4)GlcNAc(β-1,3)]nGal(β-1,4)GlcNAc(β-1,2) stramonium Man(α-1,6) (DSA) [Gal(β-1,4)GlcNAc(β-1,3)] nGal(β-1,4)GlcNAc(β-1,6) Peanut Gal Gal(β-1,3)GalNAc agglutinin (PNA) refs. 22 and 23 [Gal(β-1,4)GlcNAc(β-1,3)] nGal(β-1,4)GlcNAc(β-1,2) Man(α-1,3) Note: Datura lectin is specific for Gal-GlcNAc termini of complex oligosaccharides (22). Man(β-1,m4)GlcNAc(β-1,4)GlcNAc(β-1,N)Asn Phaseolus GlcNAc Gal(β-1,4)GlcNAc(β-1,2)Man(α-1,6) vulgaris GlcNAc(β-1,4) Man(β-1,4)GlcNAc(β-1,4)GlcNAc(β-1,N)Asn (E-PHA) Gal(β-1,4)GlcNAc(β-1,2)Man(α-1,3) erythroagglutinating phytohemagglutinin Note: A bisecting GlcNAc residue that links (β-1,4) to the β-linked mannose residue in the core is an essential and specific determinant for high-affinity binding to E-PHA-agarose column. Without this bisecting GlcNAc residue, a complex-type glycopeptide is not retained by E-PHA-agarose (24). Lectin Blotting to Detect Glycoproteins 787 (continued)
788 Table 3 Specificity of Lectins for Glycan Linked to Asparagine (N -Linked Oligosaccharide Chains) (continued) Monosaccharide Oligosaccharide Lectin specificity specificity a Phaseolus GlcNAc Gal(β-1,4)GlcNAc(B-1,2) vulgaris Man (α-1,6) (L-PHA) Gal(β-1,4)GlcNAc(β-1,6) leukoagglutinating Man(β-1,4)GlcNAc(β-1,4)GlcNAc(β-1,N)Asn phytohemagglutinin Gal(β-1,4)GlcNAc(β-1,4) Man(α-1,3) Gal(β-1,4)GlcNAc(β-1,2) Ulex europeus 1 Fuc Fuc(α-1,6) (UEA1) GlcNAc(β-1,N)Asn Note: The Gal (β-1,4) GlcNAc Man sugar sequence is essential for the binding of L-PHA (and E-PHA), as the interaction is completely abolished by the removal of the β-galactosyl residue in the peripheral portion (24). ref. 3 Lotus Fuc Fuc(α-1,6) Fuc(α-1,3) Fuc(α-1,2) tetragonolobus (LTA) GlcNAc(β-1,N)Asn Gal(β-1,4)GlcNAc Gal(β-1,4)GlcNAc refs. 3 and 25 Aleuria aurantia Fuc Fuc(α-1,6) Fuc(α-1,2) Fuc(α-1,3) (AAA) GlcNAc(β-1,N)Asn Gal(β-1,4)GlcNAc Gal(β-1,4)GlcNAc Note: The AAA lectin is particularly useful for identifying fucose bound (α-1,6) to GlcNAc. Fucose bound (α-1,6) to GlcNAc in the core region is necessary for strong binding of AAA. Fucose (α-1,3) linked to GlcNAc and fucose (α-1,2) linked to Gal (β-1,4) GlcNAc in the outer chain react only very weakly with AAA. However, fucose (α-1,3) or (α-1,2), in addition to a fucose-linked (α-1,6) to the proximal core GlcNAc enhances the binding (17,26). 788 Gravel
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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
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262 Choi, Hong, and Yoo Fig. 2. Mec
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Silver Staining of Proteins 265 33
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Silver Staining of Proteins 267 Fig
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Silver Staining of Proteins 269 3.3
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Silver Staining of Proteins 271 12.
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274 Patton plexes for colorimetric
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276 Patton device (CCD) camera. The
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278 Patton 3.2. Luminescent Detecti
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280 Patton 3.5. Luminescent Detecti
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282 Patton EDTA, pH 9.6 or using SY
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284 Patton filter. Proteins stained
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286 Patton 17. Lim, M., Patton, W.,
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288 Dunn variations in silver stain
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290 Dunn Fig. 1. A 2-DE separation
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292 Dunn 11. Stephens, R. E. (1975)
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Gels Using Eosin Y Stain 295 36 Det
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Gels Using Eosin Y Stain 297 3. An
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300 Jenö and Horst and Coomassie B
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302 Jenö and Horst Fig. 1. Side (A
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304 Jenö and Horst BT1 membrane, o
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Autoradiography and Fluorography 30
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Blotting-Electroblotting 315 PART I
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318 Page and Thorpe 4. Filter paper
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Semidry Protein Blotting 321 40 Pro
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Semidry Protein Blotting 323 2. Mem
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Discontinuous buffer systems Tris-g
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327 Table 2 Membranes Used for Elec
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Semidry Protein Blotting 329 Fig. 2
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Semidry Protein Blotting 331 Table
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Semidry Protein Blotting 333 24 h l
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Protein Blotting 335 41 Protein Blo
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Western Blotting of Basic Proteins
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344 Wisdom 4. Glutaraldehyde. 5. 50
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346 Wisdom 3. Methods 1. Dissolve 1
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348 Wisdom 3. Dialyze the modified
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350 Wisdom 6. Store the labeled ant
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352 Mao terminus. The ε-amino grou
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354 Mao conjugate with optimal modi
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356 Haugland and You Fig. 1. Struct
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358 Haugland and You Because of its
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360 Haugland and You 5. Dissolve 10
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362 Haugland and You ing with one a
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Preparation of Avidin Conjugates 36
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Staining with MDPF 375 50 MDPF Stai
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Staining with MDPF 377 transillumin
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Staining with MDPF 379 3. Alba, F.
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382 Root and Wang suspension become
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384 Root and Wang Fig. 1. Schematic
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Blots Using Direct Blue 71 387 52 D
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Blots Using Direct Blue 71 389 3.2.
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Blots Using Direct Blue 71 391 Fig.
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Immunogold 393 53 Protein Staining
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Immunogold 395 Fig. 2. Schematic re
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Immunogold 397 6. AuroProbe BLplus
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Immunogold 399 Fig. 5. Comparison o
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Immunogold 401 Table 2 Effect of Te
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Immunogold 403 15. AuroDye forte is
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Immunoblotting Using Secondary Liga
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Avidin-or Streptavidin-Biotin 415 5
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Avidin-or Streptavidin-Biotin 417 2
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Avidin-or Streptavidin-Biotin 419 R
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422 Copse and Fowler substrate to a
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424 Copse and Fowler 2. Orbital sha
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426 Copse and Fowler 4. Notes 4.1.
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428 Copse and Fowler 18. DDAO-phosp
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430 Dickinson and Fowler the advant
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432 Dickinson and Fowler 2. Membran
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434 Dickinson and Fowler Fig. 2. (A
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436 Dickinson and Fowler biotinylat
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Reutilization of Western Blots 439
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Carboxymethylation of Cysteine 453
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456 Aitken and Learmonth 11. Microd
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458 Aitken and Learmonth Table 1 El
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460 Aitken and Learmonth 4. Notes 1
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462 Ward Fig. 1. Amino acid sequenc
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Chemical Modifications of Proteins
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Chemical Modifications of Proteins
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470 Tawfik 3. Method 3.1. Nitration
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472 Tawfik preparation by pH-depend
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474 Tawfik 4. Notes 1. The concentr
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476 Tawfik 2. A molar excess of p-h
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478 Tawfik 3. Method 1. Add the gly
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480 Tawfik 3. Method 1. Dissolve th
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482 Tawfik 4. Notes 1. At neutral a
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484 Tawfik 4. Notes 1. Release of t
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486 Smith 6. Equipment includes a n
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488 Smith 3. Although the specifici
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490 Smith those bearing a prolyl re
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Cleavage at Tryptophanyl-x Bonds 49
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Alternative conditions for rapid re
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Cleavage at Tryptophanyl-x Bonds 49
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Cleavage at Aspartyl-X Bonds 499 73
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Cleavage at Aspartyl-X Bonds 501 pr
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Cleavage at Cysteinyl-x Bonds 503 7
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Cleavage at Cysteinyl-x Bonds 505 F
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Cleavage at Asparaginyl-Glycyl Bond
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Cleavage at Asparaginyl-Glycyl Bond
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Enzymatic Digestion 511 76 Enzymati
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Enzymatic Digestion 513 then remove
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Enzymatic Digestion 515 Fig. 1. In-
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Enzymatic Digestion 517 In the case
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Enzymatic Digestion 519 Another app
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Enzymatic Digestion 521 11. Modific
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524 Table 1 Digestion Buffers Recip
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526 Fernandez and Mische Fig. 1. Pe
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528 Fernandez and Mische 3. Excise
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530 Fernandez and Mische 3. The lar
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532 Fernandez and Mische membrane a
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534 Stone and Williams 2. Materials
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536 Stone and Williams In those few
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538 Stone and Williams (while maint
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540 Stone and Williams Biochemistry
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2-D TLE-TLC Mapping 543 79 Peptide
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2-D TLE-TLC Mapping 545 12. 0.25% N
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2-D TLE-TLC Mapping 547 3. Incubate
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2-D TLE-TLC Mapping 549 Table 1 Cle
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2-D TLE-TLC Mapping 551 Fig. 1. Exa
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SDS-PAGE Mapping 553 80 Peptide Map
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SDS-PAGE Mapping 555 3. Overlay sam
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SDS-PAGE Mapping 557 Fig. 1. Exampl
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560 Judd Fig. 1. Example of peptide
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Protein Hydrolysates 563 82 Product
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Protein Hydrolysates 565 2. Pronase
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Amino Acid Analysis with Marfey’s
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HPSEC 573 84 Molecular Weight Estim
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HPSEC 575 Table 1 Protein Standards
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HPSEC 577 Fig. 2. Plot of K d vs lo
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HPSEC 579 with care (see suppliers
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582 Aitken larly good resolution de
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Disulfide-Linked Peptide Detection
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Disulfide-Linked Peptide Detection
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Disulfide Bridges 589 87 Diagonal E
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Disulfide Bridges 591 3. Spot the s
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Disulfide Bridges 593 2. The moveme
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596 Aitken and Learmonth 6. Finally
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598 Aitken and Learmonth Fig. 1. (A
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600 Aitken and Learmonth 2.4. Elect
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602 Aitken and Learmonth 6. Takahas
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604 Colyer of the protein of intere
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606 Colyer 8. After 16 h of exposur
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608 Colyer stoichiometry, since it
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610 Bonenfant, Mini, and Jenö indi
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612 Bonenfant, Mini, and Jenö for
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614 Bonenfant, Mini, and Jenö incl
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616 Bonenfant, Mini, and Jenö Fig.
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618 Bonenfant, Mini, and Jenö Fig.
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620 Bonenfant, Mini, and Jenö up t
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622 Bonenfant, Mini, and Jenö 5. L
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624 Weber and McFadden Fig. 1. Sche
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626 Weber and McFadden 4. Using a p
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628 Weber and McFadden Fig. 2. Comp
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630 Weber and McFadden Fig. 4. Coom
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Protein Palmitoylation 633 93 Analy
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Protein Palmitoylation 635 Fig. 1.
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Protein Palmitoylation 637 1. Fix p
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Protein Palmitoylation 639 7. Mumby
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Fig. 1. Structure of the natural an
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644 Corsini 8. Simvastatin in its l
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646 Corsini Fig. 3. Schematic for t
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648 Corsini Table 1 Mevalonate, Pre
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650 Corsini Fig. 5. Metabolic label
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652 Corsini Fig. 7. Two-dimensional
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654 Corsini 7. When prenylated prot
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656 Corsini 24. Danesi, R., McLella
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658 Andres et al. Fig. 1. Proposed
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660 Andres et al. Fig. 2. SDS-PAGE
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662 Andres et al. Fig. 4. Chromatog
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664 Andres et al. Fig. 6. Specific
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666 Andres et al. 10. Residual orga
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668 Andres et al. 2. The metabolica
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670 Andres et al. 3. Clarke, S. (19
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Phosphopeptide Mapping 673 96 2-D P
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Phosphopeptide Mapping 675 3. Add 1
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Phosphopeptide Mapping 677 Fig. 1.
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Phosphopeptide Mapping 679 until th
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Protein Mutations by MS 681 97 Dete
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Protein Mutations by MS 683 protein
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Protein Mutations by MS 685 Fig. 2.
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Protein Mutations by MS 691 Fig. 10
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Nanoelectrospray MS/MS for Peptide
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MALDI-MS for Protein Identification
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Page 713 and 714: MALDI-MS for Protein Identification
Page 715 and 716: Protein Ladder Sequencing 733 100 P
Page 717 and 718: Protein Ladder Sequencing 735 Prote
Page 719 and 720: Protein Ladder Sequencing 737 3. Ex
Page 721 and 722: Protein Ladder Sequencing 739 2. Wa
Page 723 and 724: 742 Hennig sequences (see Subheadin
Page 725 and 726: 744 Hennig In the age of genomics,
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Page 729 and 730: 748 Spencer and Davie Fig. 1. Two-d
Page 731 and 732: 750 Spencer and Davie 4. Notes 1. T
Page 733 and 734: Proteins Cross-linked to DNA by For
Page 739 and 740: Glycoprotein Detection 761 104 Dete
Page 741 and 742: Glycoprotein Detection 763 Schiff
Page 743 and 744: Glycoprotein Detection 765 3.1.1. G
Page 745 and 746: Glycoprotein Detection 767 Table 1
Page 747 and 748: Glycoprotein Detection 769 5. Resus
Page 749 and 750: Glycoprotein Detection 771 Fig. 1.
Page 751 and 752: Detection of Glycosylated Proteins
Page 757 and 758: 780 Gravel Fig. 1. Glycoprotein blo
Page 759 and 760: 782 Gravel Fig. 3. Glycoprotein blo
Page 761 and 762: 784 Table 1 Glycans N-Glycosidicall
Page 763: 786 Table 3 Specificity of Lectins
Page 767 and 768: 790 Gravel dimethylformamide. These
Page 769 and 770: 792 Gravel 3. Montreuil, J., Bouque
Page 771 and 772: 794 Gravel
Page 773 and 774: 796 Goodarzi, Fotinopoulou, Turner
Page 781 and 782: 804 Hounsell, Davies, and Smith 2.
Page 785 and 786: Monosaccharide Analysis by GC 809 1
Page 787 and 788: Linkage and Substitution Patterns 8
Page 789 and 790: Linkage and Substitution Patterns 8
Page 795 and 796: 820 Hounsell, Davis, and Smith 6. T
Page 799 and 800: 824 Mizuochi and Hounsell 3. Method
Page 801 and 802: 826 Mizuochi and Hounsell Reference
Page 809 and 810: 834 Weitzhandler et al. alditols (1
Page 811 and 812: 836 Weitzhandler et al. Fig. 1. HPA
Page 813 and 814: 838 Weitzhandler et al. 2. Add 0.1
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Microassay of Protein Glycosylation
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Carbohydrate Electrophoresis 851 12
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Carbohydrate Electrophoresis 853 2.
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Carbohydrate Electrophoresis 855 Pl
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Carbohydrate Electrophoresis 859 Fi
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Carbohydrate Electrophoresis 861 wa
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866 Merry blly less expensive than
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868 Merry 8. Whatman no. 3 chromato
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870 Merry 4. Dialyze for a minimum
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872 Merry 9. Leave for 5 min and un
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874 Merry 2. Column: Reverse-phase
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Table 1 Incubation Conditions for E
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878 Merry 3.7. Exoglycosidase Diges
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880 Merry Fig. 6. Example of exogly
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882 Merry 17. Rice, K. G., Takahash
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Glycoprofiling and SPR 885 124 Glyc
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Glycoprofiling and SPR 887 2. Mater
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Glycoprofiling and SPR 889 Fig. 3.
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Glycoprofiling and SPR 891 α2-3 Ne
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894 Turnbull Fig. 1. Basic principl
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896 Turnbull 13. Enzyme buffer (0.2
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898 Turnbull Table 1 Exoenzymes for
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900 Turnbull Fig. 3. IGS of a hepar
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902 Turnbull 4. Notes 1. Using larg
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904 Turnbull 20. Rice, K., Rottink,
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906 Hooker and James 3. High-perfor
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908 Hooker and James Fig. 1. Whole
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910 Hooker and James at individual
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912 Hooker and James Fig. 4. Sialyl
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914 Hooker and James 16. Ashton, D.
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Lectin Affinity Chromatography 917
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Antibody Production 935 128 Antibod
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Antibody Production 937 1.1. Donor
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Antibody Production 939 2. Material
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Production of Anitbodies Using Prot
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Production of Anitbodies Using Prot
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Production of Polyclonal Antibodies
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Peptide Conjugation and Immunizatio
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964 Bailey is oxidized by chloramin
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The Lactoperoxidase Method 967 133
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The Bolton and Hunter Method 969 13
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Radioiodination Using IODO-GEN 971
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980 Bailey 3. Specific antiseum to
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982 Bailey Amount of radioactivity
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984 Page and Thorpe 2. Centrifuge s
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DEAE-Sepharose Chromatography 987 1
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IgG Purification with Ion-Exchange
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PEG Precipitation 991 141 Purificat
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994 Page and Thorpe 2. Materials 1.
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996 Dolman and Thorpe Fig. 1. Typic
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Antigen-Ligand Columns 999 144 Puri
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Antigen-Ligand Columns 1001 4. When
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1004 Page and Thorpe 7. Filter and
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1006 Page and Thorpe Fig. 1. SDS-PA
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Purification of IgY from Chicken Eg
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Purification of IgY from Chicken Eg
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1014 Fassina et al. limit the use o
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1016 Fassina et al. 2. Materials Ta
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1018 Fassina et al. 10. Filter the
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1020 Fassina et al. 1. Dilute sampl
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1022 Fassina et al. analysis indica
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1024 Fassina et al. 6. Khayam-Bashi
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1026 Hammerl et al. down, with the
Page 987 and 988:
1028 Hammerl et al. 1. Clean glass
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1030 Hammerl et al. Fig. 1. Experim
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1032 Hammerl et al. can “corrode
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Single-Chain Antibodies 1035 150 Ba
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Single-Chain Antibodies 1037 ing th
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Single-Chain Antibodies 1039 6. Mag
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Single-Chain Antibodies 1041 XL1-Bl
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Single-Chain Antibodies 1043 fore,
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Single-Chain Antibodies 1045 16. Ho
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Enzymatic Digestion of MAbs 1047 15
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Enzymatic Digestion of MAbs 1049 2.
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Enzymatic Digestion of MAbs 1051 2.
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Making Bispecific Antibodies 1053 1
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Making Bispecific Antibodies 1057 F
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Phage Display 1059 153 Phage Displa
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Phage Display 1061 5000, 1 mL of 2-
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Phage Display 1063 11. Agarose top:
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Phage Display 1065 3.1.3.2. AFFINIT
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Phage Display 1067 8. Shake vigorou
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Phage Display 1069 4. Notes 1. Fila
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Phage Display 1071 9. Sengupta J.,
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Selection by Panning 1073 154 Scree
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Selection by Panning 1075 Fig. 1. F
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Selection by Panning 1077 12. Centr
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Selection by Panning 1079 4. Notes
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Selection by Panning 1081 33. The
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Antigen Measurement Using ELISA 108
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Enhanced Chemiluminescence 1089 156
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Enhanced Chemiluminescence 1091 Tab
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Enhanced Chemiluminescence 1093 is
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Enhanced Chemiluminescence 1095 lig
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Immunoprecipitation 1097 157 Immuno
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Immunoprecipitation 1099 Table 2 Pr
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Immunoprecipitation 1101 oligosacch
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Immunoprecipitation 1103 6. Very ge
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Immunoprecipitation 1105 2. Dry the
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Short Chapter Title 1107 PART VIII
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1110 Page and Thorpe final quantity
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1112 Page and Thorpe 2. Materials 1
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161 From: The Protein Protocols Han
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162 From: The Protein Protocols Han
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Affinity Purification of Monoclonal
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An Efficient Method for MAb Product
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Index 1139 Index A Absorbance (UV),
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Index 1141 Electrophoresis of antib
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Index 1143 of glycoproteins, 905-91
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Index 1145 India ink, 338 lectin st
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The Protein Protocols Handbook Seco
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