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30 Yip and Hutchens 7. Hutchens, T. W. and Yip, T. T. (1990) Differential mteracuon of pepndes and protem surface structures with free metal ions and surface-immobilized metal ions.J. Chromutogx 500,531~542. 8. Sulkowskr, E. (1985) Purification of proteins by IMAC. Trends Biotechnol 3, l-7. 9. Hutchens, T. W. and Li, C. M. (1988) Estrogen receptor mteracnon with immobihzed metals: Differential molecular recogniuon of Z&, Cu2+, and Ni2+ and separation of receptor isof0rms.J. Mol. Recog. 1, 80-92. 10. Hutchens, T. W., Li, C. M., Sato, Y., and Mp, T.-T. (1989) Multiple DNA- bmdmg estrogen receptor forms resolved by mteracuon with rmmobihzed metal ions. Identificatron of a metal-bmdmg domain. J Baol . Chem. 264, 17,206-17,212. 11. Hemdan, E. 8, Zhao, Y.-J., Sulkowslu, E., and Porath, J. (1989) Surface to pography of histtdme residues: A facile probe by immobihzed metal ion affimty chromatography. Proc. Nat1 Acad. Sn. USA 86, 1811-1815. 12. Hutchens T. W. and Yip, T.-T. (1991) Metal hgand-induced alterahons m the surface structures of lactofernn and transferrm probed by mterachon with immobihzed Cu(II) 1ons.j Chromatogr. 536, 1-15. 13. Mantovaara-Jonsson, T., Pertoft, H., and Porath, J. (1989) Purihcauon of human serum amyloid ccmponent (SAP) by calcium affmty chromatography. Bzotechnol. A#. Biochem. 11, 564-571. 14. Hutchens, T. W., Nelson, R. W., Li, C. M., and Yip, T.-T. (1992) Synthetic metal binding protem surface domains for metal ion-dependent mter-ac- bon chromatography. I. Analysis of bound metal ions by matrix-assisted W laser desorpuon urn-f-flight mass spectrometry. J. Chromutogr. (m press). 15. Hutchens, T. W. and Yip, T.-T. (1992) Immobihzauon of syntheuc metal- bmdmg pepudes derived from metal ion transport proteins. II. Buddmg models of btoacttve protem surface domam structures. j. chnrmatogr. (m press). 16. Hutchens, T. W. and Yip, T.-T. (1990) Protein mteracuons with immobilized transition metal ions: Quantitative evaluations of variations in affimty and binding capacity. Anal. Biochem. 191, 160-168. 17. Nakagawa, Y., Yip, T. T., Belew, M., and Porath, J. (1988) High performance immobilized metal ion affimty chromatography of pepudes: Analytical separation of biologically active synthetic pephdes. Anal. Bzochem. 168, 75-81. 18. Fanadi A.J. (1987) Afhmty chromatography and metal chelate afhmty chro matography. CRC Cntzcal Rev. Anal. Chem. 18, l-44. 19. Kagedal, L. (1989) Immobihzed metal ion affuuty chromatography, m Hzgh Resolutaon Protan Pur@cation (Ryden, L. and Jansson, J.-C., eds.), Verlag Chemie Inst., Deerfield Beach, FL, pp. 227-251. 20. Hutchens, T. W., Yip, C., Li, C. M., Ito, K., and Komiya, Y. (1990) Ligand effects on estrogen receptor interaction with immobihzed Zn(I1) ions. A comparison of unliganded receptor with estrogen-receptor complexes, and anuestrogen-receptor complexes. submitted.
Immobilized Metal Ion Interaction 31 21. Muszynska, G., Zheo., Y.-J., and Porath, J. (1986) Carboxypepbdase A: A model for studymg the mteraction of proteins with lmmobdlzed metal Ions. J Inorg. Baochem. 26, 127-135. 22. Yip, T.-T. and Hutchens, T. W. (1991) Metal ion affhuty adsorption of a ZN(II)-Transport protein present m maternal plasma dunng lactation: Stt-uc- tural characterization and ldentlficatlon as hlsbdme-rich glycoprotem. Pw tetn Exfnx.sswn ad Punjcataon 2,3X5-362. 23. Hutchens, T. W., Nelson, R. W., and Yip, T.-T. (1992) Recognition of transition metal ions by peptldes: Identification of specific metal-binding pep bdes m proteolyk digest maps by UV laster desorphon time-of-flight spectrometry. FEBS I.-&t. (m press). 24. Hutchens, T. W., Nelson, R. W., and Yip, T.-T. (1991) Evaluation of pep tide-metal ion mteractlons by W laser desorphon time-of-flight mass spectrometry. J. Mol. I&cog. 4, (m press). 25. Hutchens, T W., Nelson, R. W., Allen, M. H., Li, C. M., and Mp, T.-T. (1992) Peptide metal ion mteractions m solution: Detection by laser desorphon time-of-flight mass spectrometry and electrospray lomzahon mass spectrometry. Baol. Mass Spectrom. (m press). 26. Hutchens, T. W. and Yip, T.-T. (1991) Protein mteracaons with surface- lmmobdlzed metal ions: Structuredependentvanations m affinity and bmdmg capacity constant with temperature and urea concentration. J Inorg. Bzoch..em. 42, 105-l 18. 27. Flgueoroa, A., Corradml, C., Felbush, B., and Karger, B. L. (1986) High- performance lmmoblhzed metal ion afflmty chromatography of proteins on lmmodlacetic acid sihca-based bonded phases.J; chromatogr. 371,335-352. 28. Hutchens, T. W., Yip, T.-T., and Porath, J. (1988) Protein interaction wth lmmoblhzed hgands. Quantitative analysis of eqmhbnum parhbon data and comparison with analytical alXnity chromatographlc data using lmmoblhzed metal ion adsorbents. Anal. Bzochem. 170, 168-182. 29. Hutchens, T. W., and Ll, C. M. (1990) Llgand-bmdmg properties of e&-cl gen receptor proteins after interaction with surface-immobhzed Zn (II) ions: Ewdence for locahzed surface interachons and mmlmal conformahonal changes. J. Mol. Recog. 3, 174-l 79.
Page 1 and 2: Thiophilic Adsorption Chromatograph
Page 3 and 4: Thiophilic Adsorption 3 8. Methanol
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Page 45 and 46: &AP!t’ER 4 Boronic Acid Matrices
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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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