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44 Vijayalakshmi cental IgG. The histamine-coupled gel retained a much higher amount of IgG, but the specificity to IgGl was enhanced with the imidazole (15). References 1. Vijayalakshmi, M. A. (1989) Pseudobiospecific hgand affinity chromatography. Tibtech 7(3), 71-76. 2. Lehninger, A. L. (1976) Bs&errzrstly. Worth, New York, 230,231. 3. Kanoun, S., Amourache, L., Knshnan, S., and Vijayalakshm:, M. A. (1986) A new support for the large scale purificauon of proteins. J Chromatogr. 376,259-267. 4. Hjalmarsson, S. and Akesson, R. (1983), Modern Kjeldahl procedure. ht. Lab. 70-76. 5. Chang, S. H., Goodmg, K. M., and Regmer, F. E. (1976) Use of oxuanes m the preparation of bonded phase supports. J# Chromutogr. 120,321-333. 6. Sundberg, L. and Porath, J. (1974) Preparation of adsorbents for biospecific affinity chromatography. 1. Attachment of ammo group containing hgands to insoluble polymers by means of biinctional 0xuanes.J. chnrmatogr 90,87-98. 7. Kanoun S. (1988) Contrrbuuon 4 la chromatogmphie de pseudo-afhmt& Modele de proteines: Les immunoglobuhnes G placentaires. PhD Thesis, University of Compiegne, 95-99. 8. Amourache, L. and Vrjayalakshmi, M. A. (1984) Aflimty chromatography of kid chymosm on hisudyl-sepharose. J Chromatogr. 303, 285-290. 9. Mehn, S. and Vqayalakshmi, M. A. (1987) Zonal eluuon analysis of IgG retention on histidyl-sepharose. BioL Uwm. Ho@e-S#ds 368 (7), 762. 10. Krishnan, S., Gaehel-Vignais, I., and Viiayalakshnu, M. A. (1987) A semi- preparative isolation of carboxypepudase. Isoenzymes from A$er@lus Nzger by a angle immobilized metal ion affimty chromatography. J. Chromatogr 397,339-346. 11. Vijayalakshmi, M. A. and Thomas, D. (1985) Affimty chromatography as a production technque. l7te World Bwted. Rtpnt online 1 (Europe), 131-140. 12. Cabrera, K. E. and Wilchek, M. (1987) Coupling of hgands to primary hy- droxyl contammg silica for high performance affimty chromatography. J. Chronuztogrs 397,187-196. 13. Akoum, A., Viiayalakshmi, M. A., Car-don, P., Fournet, B., !&got, M., and Guespm-Michel, J. F. (1987) My xococcus xanthus produces an extracellular glycopepude that displays blood anucoagulant properties. Ens. Mzcrob. TechnoL 9, 426429. 14. Akoum, A., Qayalakshmi, M. A., and &got, M. (1989) Scale-up of “Myxalme” purification by a pseudo-affintty method usmg a radial flow column. Chromatographia 28, 157-160. 15. Elkak, A. and Vqayalakshmi, M. A. (1991) Study of the separation of mouse monoclonal antibodies by pseudobioaffimty chromatography using matnx- linked hisudine and h1stamme.J. Chromatogr. 570, 29-41.
&AP!t’ER 4 Boronic Acid Matrices for the Affinity Purification of Glycoproteins and Enzymes James H. Hageman and Glenn D. Kuehn 1. Introduction Boronic acids immobilized on insoluble matrices have been used for over a decade to purify proteins and enzymes (1,2). Boronic acid matrices have been used to purify: 1. Glycoproteins, 2. Enzymes for which a boronic acid moiety is an inhibitor, and 3. Enzymes that bind to specific dial-containing cofactors (such as UTP or NADP+). In all instances, the mechanisms by which the purifications are achieved are presumed to involve the unique capacity of boronic acids to bind reversibly to biomolecules bearing dials. The great recent success of boronic acid matrices in clinical screening for elevated levels of glycosylated hemoglobin, which occur in diabetes melitus, may give some impetus for extending the use of these materials in the purification of glycoproteins generally. Because of the rela- tive recency of boronate-matrix chromatography and our belief that the methods described will be of wide applicability, we give below a larger introduction than is usual for this series. In aqueous solutions, the only stable complex formed between diols, such as neutral sugars and boronic acids, is that of the boronate From Methods m Molecular Brology, Vol 17. Pracbcal Pro&n Chromatography Edlted by. A. Kenney and S. Fowell Copynght 0 1992 The Humana Press Inc., Totowa, NJ 45
Page 1 and 2: Thiophilic Adsorption Chromatograph
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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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