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14 Hutchens References 1. Hutchens, T. W. and Porath, J. (1986) Thiophihc adsorption of immunoglobuhns-Analysis of conditions ophmal for selecuve immobihzation and punficauon. Anal. Bzochem. 159,217-226. 2. Cohn, E. J., Strong, L. E., Hughes, W. L. Jr., Mulford, D. J., Ashworth, J, N., Mehn, M., and Taylor, H. L. (1946) Preparation and properties of serum and plasma proteins. IV. A system for the separauon mto fractions of the protein and lipoprotein components of biological ussues and flu1ds.J. Am. Chm. Sot. 68, 459-473. 3. Hlelm, H., Hlelm, K., and SJoquist,J. (1972) Protein A from staphylococcus aureus. Its isolauon by affhnty chromatography and its use as an affmity adsorbent for isolation of immunoglobuhns FEBS L&t. 28, 73-76. 4. RoqueBarreira, M. C., and Campos-Neto, A (1985) Jacahn: An IgA-bmd- ing lectin. J Immunol. 134,1740-l 743. 5. Regmer, F. E. (1988) Liqmd chromatography of immunoglobuhns. LGGC 5,962-968. 6. Hutchens, T. W., Magnuson, J. S., and Yip, T.-T. (1989) Selective removal, recovery and chamcterizahon of immunoglobulms from human colostrum. Pedaatr. Res. 26, 623-628.7. 7. Hutchens, T. W., Magnuson, J. S., and Yip, T.-T. (1990) Secretory IgA, IgC, and IgM immunoglobulins isolated simultaneously from colostral whey by selective thiophrhc adsorpuon. J Immunol. Methods 128, 89-99. 8. Nopper, B., Kohen, F., and Wilchek, M. (1989) A thiophillc adsorbent for the one-step high-performance liquid chromatography purification of monoclonal antibodies. Anal. Bzochem. 180, 66-71. 9. Hutchens, T. W. and Porath, J. (1987) Protein recogmuon m immobihzed ligands: Promotion of selective adsorption. C&z. Ch. 33, 1502-1508. 10. Porath, J. and Hutchens, T. W. (1987) Thiophihc adsorption: A new kmd of molecular mteraction. I&J; Qua&. C&IZ @ant. Bzol Symp. 14,297-315. 11. Porath, J., Maisano, F., and Belew, M. (1985) Thiophihc adsorptlon-a new method for protein fractionation. FEBS L&t. 185,306-310. 12. Hutchens, T. W. and Porath, J. (1987) Tmophihc adsorption. A compari- son of model protein behavior. Bzochemastly 26, 7199-7204. 13. Bradford, M. M. (1976) A rapid and sensitive method for the quanhtauon of micrgram quanuues of protein utilizmg the principle of protemdye bmd- ing. Anal. Baochem. 72,248-254. 14. Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallra, A. K., Gartner, F. H., Provenzano, M. D., Fulimoto, E. K., Goeke, N. M., Ohlson, B. J., and Klenk, D. C. (1985) Measurement of protein using bicmchonmic acid. Anal. Baochem. 150, 76-85. 15. Redinbaugh, M. G. and Turley, R. B. (1986) Adaptauon of the bicmchonimc acid protein assay for use with microtiter plates and sucrose gradient fractions. Anal. Biochem. 153, 267-271. 16. Laemmh, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227,680-685.
Thiophilic Adsorption 15 17. Morrissey, J. M. (1981) Silver stam for protems m polyacrylanude gels: A modified procedure wrth enhanced uniform sensrnvrty. Anal. Bzochem. 117, 307-310. 18. Larsson, P.-O., Glad, M., Hansson, L., Mansson, M.-O., Ohlson, S., and Mosbach, K. (1983) High-performance hqurd chromatography. Adv. Chromatogr. 21, 41-85. 19. Axen, R., Drevm, H., and Carlsson, J. (1976) Preparation of modified agar- ose gels contammg throl groups. Acta Chem. Stand. 82, 471-474. 20. Ellman, G.L. (1959) Tissue sulfhydryl groups. Arch. Bzochem. Bzophys. 82, 70-77. 21. Hawkes, R., Nrday, E., and Gordon, J. (1982) A dot-rmmunobmdmg assay for monoclonal and other anubodles. Anal. Bzochem. 119, 142-147. 22. Towbm, H., Staehelm, T., and Gorden, J. (1979) Electrophoreuc transfer of protems from polyaclylamrde gels to mtrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
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Page 33 and 34: CHAF’TER 3 Histidine Ligand Affin
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Page 45 and 46: &AP!t’ER 4 Boronic Acid Matrices
Page 47 and 48: Table 1 Types of Sold Matrices That
Page 49 and 50: Boronic Acid Matrices 49 amide, aga
Page 51 and 52: Boronic Acid Matrices 51 Table 3 Bm
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Boronic Acid Matrices 65 rylamide g
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Boronic Acid Matrices 67 Sephadex,
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Boronic Acid Matrices 69 30. Plzer,
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Boronic Acid Matrices 71 61. Hjerte
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74 Battey and Venis 2. Materials 1.
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76 Battey and Venis strained throug
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78 Battey and Venis Fig. 2. SDS-PAG
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80 Battey and Venis 6. Laemmh, U. K
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Lectm Concanavahn A (tin A) L.kms c
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84 West and Goldring 2. Materials 2
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86 West and Goldring 6. Wash the co
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88 West and Gbldring 4. Sharma, S.
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CHAPTER 7 Dye-Ligand Affinity Chrom
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Dye-Ligand Chromatography 93 B Fig.
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Dye-Ligand Chromatography 95 the eq
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Dye-L&and Chromatography 20 A,,, 1.
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Dye-Ligand Chromatography 99 leakag
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Dye-Ligand Chromatography or most o
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Dye-Ligand Chromatography 103 6. Sm
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106 Clonis tion in the size of the
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support Sdica, unmodified Hypersll
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110 Clonis 2. Materials 2.1. Coatin
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112 Clonis 6. Hydrochloric acid (1
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114 Clonis 2.3.2. Separation of BSA
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116 Clonis 3.1.4. Preparation of Al
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116 Clonis 3.2.4. Immobilization of
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120 Clonis TiME (m(n) - Fig, 1. Res
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122 Clonis 5. The carbodiimide-prom
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Immunoafflnity Chromatography Georg
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Immunoafinity Chromatography 127 OC
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Immunoafinity Chromatography 129 3.
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Immunoafinity Chromatography 131 3.
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Immunoafinity Chromatography 133 ho
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136 Pepper Table 1 Polyclonal Antib
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138 Pepper to see which functions b
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140 Pepper role in diagnosing probl
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142 Pepper Fig. 1. ELISA (A,B), RIA
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144 Pepper mum bound signal of 40%
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146 Pepper 10 30 50 70 90 110 130 1
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148 Pepper radioactive decay, the c
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150 AEl0 ELISA loo 10’ lo2 lo3 lo
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152 Pepper subclassed antibodies, w
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154 Pepper binding. Wash three time
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156 I A ANTMOOV AB3 (I$ =l xd”) B
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158 Pepper 3.4. Eluant Selection an
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160 Pepper tion reagents (18,44), w
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162 Pepper directly by adding a 125
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164 Pepper ant/gel are not very com
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Pepper ‘7. There are a number of
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168 Pepper 5. Miller, K. F., Bolt,
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170 Pepper 35. Lamoyi, E. and Nison
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&LWI’ER 11 Some Alternative Coupl
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Alternative Coupling Chemistries 17
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CHAPTER 12 Exploiting Weak Affiniti
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Exploiting Weak Affinities 199 The
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Exploiting Weak Affinities 201 4 Co
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Exploiting Weak Affinities 203 a P
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-me Trade name Matrix Aldehyde Chlo
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Exploiting Weak Affinities 207 prof
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CHAPTER 13 Biospecific Affinity Elu
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Biospecific Affinity El&ion 211 mol
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Biospecific Affinity E&ion 213 stre
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Biospecijic Affinity Elution 215
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Biospecific Affinity Elution 217 0
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Blospectjic Affinity El&ion 219 thr
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Biospecific Affinity Elution 221 th
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224 Harris In considering applicati
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226 Harris pressures (10-40 bar) re
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228 Table 2 Cahbrahon Protems Suita
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230 Harris time (min) Fig. 2. Const
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232 Harris guard and/or separation
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234 Harris 15 20 25 time after inje
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236 Harris References 1. KopacieMnc
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238 Li and Hutchens This chapter pr
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240 Li and Hutchens !=RACl-lON NUMB
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242 Li and Hutchens Desired pH grad
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244 Li and Hutchens sample volume s
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9 6 Li and Hutchens 0 20 40 60 80 1
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248 Li and Hutchens of a focusmg bu
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250 Kenney DEAE SP CM QA PEI CBX Ta
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Table 2 Some Commercially Available
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254 Kenmy b. Gradient former (see N
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is eluted last from the cation exch
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Kenney bacteria and spores. This ki
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260 Cramer displacer front. The dis
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1.1. Methods Development in Displac
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264 Cramer I I I I I I I I I I I I
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266 Cramer obtained using the mathe
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268 Cramer during the introduction
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270 Cramer Problem Typical Problems
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Purification of DNA Binding Protein
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288 Sherwood Table 1 General Techni
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290 Sherwood risk of product proteo
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292 Sherwood ing 8000g and with a b
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Organrsm Endma chtysanthemz PSeUdo?
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296 Sherwood Table 5 Effect of Ioni
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298 Sherwood 2.1. Filtration Concen
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300 Sherwood 2.2.1. Precipitation b
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302 Sherwood Precipitate can be rem
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304 Sherwood 5. Hammond, P. M., Ram
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CHAFFER 20 Determination of Purity
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Purity and Yield 309 reason is that
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Purity and Yield 311 (l-3 mm thick)
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Purity and Yield 313 is phosphomoly
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Purity and Yield 315 A Acetyl CoA-
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Purity and Yield 317 3 MM filter pa
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Purity and Yield 319 Solution A, So
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Purity and Yield 321 ide solution.
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Purity and Yield 323 11. Layne, E.
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