Biochromatography : theory and practice

Biochromatography: Theory and practice......Page 2
Contents......Page 5
Contributors......Page 7
Acknowledgements......Page 10
Preface......Page 11
Foreword......Page 13
Choice of sources of raw materials......Page 15
Extraction methods......Page 16
Fractionation techniques......Page 18
Organisation of different chromatographic steps in the protein fine purification......Page 20
Monitoring the fractionation and purification......Page 21
References......Page 22
Separation principle......Page 23
Pore volume/size......Page 25
Particle size......Page 26
Silica......Page 27
Solvent......Page 28
Flow rate......Page 29
Sample volume......Page 30
Analytical gel filtration......Page 31
Fractionation......Page 33
Desalting......Page 34
References......Page 35
Matrices and ion exchange groups......Page 38
Porosity......Page 40
Particle size......Page 41
Ion exchange mechanism......Page 42
Mass transfer mechanism......Page 43
Protein separation on ion exchangers......Page 44
Classical ion exchange chromatography......Page 46
Special aspects of ion exchange chromatography......Page 47
Scaling up of ion exchange chromatography......Page 49
Columns vs batches......Page 50
Matrix deterioration......Page 53
Cleaning processes for ion exchangers......Page 54
References......Page 56
Reversed-phase vs hydrophobic Interaction chromatography......Page 59
The CNBr procedure......Page 60
Hydrophobic non-charge-free gels \0一䌀䘀ⴀ最攀氀猀......Page 62
Charge containing \0一䌀䘀 versus charge-free \0䌀䘀 hydrophobic gels......Page 63
The chain-length parameter......Page 64
Multivalence......Page 65
Salting-out on unsubstituted hydrophilic gels......Page 68
Salting-out and salting-in on hydrophobic gels......Page 70
Theories of salt actions on proteins......Page 72
Introduction......Page 73
The critical-hydrophobicity procedure......Page 74
One-step purification of native fibrinogen from human blood plasma......Page 76
Conclusions......Page 77
References......Page 78
Introduction......Page 84
Dependence of log k on psi and log k on......Page 87
Dependence of log k and log k on temperature at fixed values of psi or......Page 91
Dependence of log k and log k on temperature at different values of psi or......Page 93
Dependence of S and log k0 values on temperature and psi or......Page 99
Behaviour of polypeptides with preferred secondary structures: general comments......Page 103
Behaviour of beta-endorphin and neuropeptide Y: prototype examples of the retention behaviour of alpha-helical polypeptides......Page 104
Beta-endorphin......Page 105
Neuropeptide Y......Page 107
Behaviour of gramicidin analogues: prototype examples of the behaviour of beta-sheet polypeptides......Page 118
The effect of temperature on the RP-HPLC behaviour of intermediate molecular weight globular proteins: myoglobin, hen egg white lysozyme and cytochrome c......Page 119
Observations on the origin of the non-linear van’t Hoff behaviour of polypeptides and proteins in hydrophobic RP-HPLC environments......Page 124
Bandwidth dependencies and the participation of interconverting intermediates of polypeptides and proteins in dynamic RP-HPLC systems......Page 134
Conclusions......Page 145
Glossary of terms and symbols......Page 146
References......Page 148
Introduction......Page 153
General principles of affinant-substance recognition......Page 154
Required characteristic......Page 164
Cellulose and its derivatives......Page 167
Dextran gels......Page 169
Agarose and Its derivatives......Page 170
Acrylamide derivatives......Page 173
Methacrylate supports......Page 175
Polystyrene and its derivatives......Page 177
Combination of biopolymers with synthetic polymers......Page 178
Inorganic supports......Page 179
Controlled pore glass......Page 180
Porous and nonporous silica......Page 181
Iron and nickel oxides......Page 182
Membranes and tubes......Page 183
Effect of the nature of proteins and solid supports......Page 185
Epoxide-containing supports......Page 186
Hydrazide derivatized solid supports......Page 188
Periodate oxidation......Page 191
Glutaraldehyde activation technique......Page 193
Cyanogen bromide activation......Page 195
Coupling with condensation agents......Page 196
Activation with carbonylating reagents......Page 198
Reversible covalent immobilization of proteins by thiol-disulphide interaction......Page 201
Benzoquinone activation......Page 202
Blocking of unreacted groups and washing out of noncovalently bou and ligands: recommendations......Page 204
General considerations in the choice of sorbents, coupling and blocking procedures......Page 206
Biotin and avidin or streptavidin......Page 208
Oriented immobilization of immunoglobulin G by use of Protein A......Page 210
Biospecific complex formations of enzymes......Page 212
Classical affinity chromatography......Page 213
High-performance liquid affinity chromatography......Page 214
Immobilization of enzymes on their immunosorbents......Page 215
Conclusion......Page 223
References......Page 224
Alternative dyes......Page 232
Some personal observations and developments......Page 234
Purity, reproducibility and availability of dye adsorbents......Page 236
Protocols for developing a dye ligand step in a protein purification procedure......Page 237
Other affinity methods using dyes......Page 239
References......Page 240
Structure and chemistry of triazine dyes......Page 242
Synthesis and purification of triazine dyes......Page 244
Preparation of a dye adsorbent......Page 245
Dye screening: selection of dyes as ligands for affinity chromatography......Page 248
The development and optimization of a protein purification, based on dye-ligand adsorbents......Page 250
Large-scale dye-ligand affinity chromatography......Page 251
Purpose-designed dye-ligands: the generation of biomimetic dye-ligands......Page 252
References......Page 256
Introduction......Page 259
Selection of matrices for ligand immobilization......Page 260
Influence of support matrix......Page 261
Choice of coupling chemistry......Page 263
Influence of spacer arm......Page 265
Influence of ligand orientation......Page 266
Adsorption conditions: a critical step in HLAC......Page 267
Importance of the upstream extraction methods......Page 268
Influence of buffer composition......Page 269
Role of adsorption temperature......Page 271
Influence of additives: salt and chaotropic agents......Page 272
Example of a combination of these elution parameters......Page 273
What is the basis for the selective retention of proteins on immobilized histidine?......Page 274
Specificity of the recognition sites in proteins?......Page 275
References......Page 276
Introduction......Page 279
Support matrices......Page 280
Choice of the chelating groups......Page 281
Metal ions and adsorption center......Page 282
Peptide/protein structure......Page 283
The influence of solvent composition......Page 285
Solvents preparation......Page 287
Column packing......Page 288
Clues to IMAC/selectivity......Page 289
Defining the size of the spherical probe......Page 290
IMA in the Electrokinetic Chromatographic mode......Page 293
References......Page 296
Molecular structure of the thiophilic ligand and the effect of different matrixes......Page 301
Studies of thiophilic gels based on heterocycles......Page 303
Mechanisms of thiophilic interaction......Page 304
Applications......Page 305
Secretory IgA, IgG and IgM immunoglobulins isolated simultaneously from colostral whey by selective thiophilic adsorption Hutchens et al., 1989......Page 306
Purification of monoclonal antibodies \0䈀攀氀攀眀 攀琀 愀氀⸀Ⰰ ㄀㤀㠀㜀......Page 307
Purification of Fab2 and Fc fragments of IgG1 antibodies from murine ascitic fluid Yurov et al., 1994......Page 309
References......Page 311
Introduction......Page 313
Secondary interactions......Page 314
Boronate ligands......Page 315
Carbohydrates......Page 317
Glycoproteins and enzymes......Page 318
Other small molecules......Page 319
References......Page 320
Concept of polymer shielding......Page 324
Suitable polymers for shielding......Page 326
Strategy......Page 327
Applications of polymer shielding in expanded bed chromatography......Page 328
References......Page 333
Biological role of glycans......Page 334
Molecular pathology of glycoproteins......Page 335
Monosaccharide constituents......Page 336
MICROHETEROGENEITY OF GLYCANS?THE GLYCOFORMS......Page 337
O-GLYCOSYLPROTEIN GLYCANS \0伀ⴀ䜀䰀夀䌀䄀一匀......Page 338
Overview of the methodology of glycan isolation and primary structure determination......Page 342
Problems of lectin specificity......Page 343
Determination of the “complex” specificity of lectins......Page 344
Specificity of lectins towards complex oligosaccharides......Page 345
LECTINS IDENTICAL IN TERMS OF MONOSACCHARIDE SPECIFICITY CAN PRESENT DIFFERENT COMPLEX SPECIFICITY......Page 349
IMPORTANCE OF THE SPATIAL CONFORMATION OF GLYCANS IN THE INTERACTION WITH LECTINS......Page 350
OTHER COUPLING METHODS FOR IMMOBILIZATION OF LECTINS......Page 351
USE OF CROSSED AFFINOIMMUNOELECTROPHORESIS CAIE OF GLYCOPROTEINS AS A GUIDE FOR LECTIN AFFINITY CHROMATOGRAPHY......Page 352
BINDING CAPACITY OF THE IMMOBILIZED LECTINS AND PROBLEMS OF THE ELUTION......Page 353
Protocol for affinity chromatography of glycoproteins on immobilized ConA......Page 354
Use of immobilized lectins for fractionation of glycopeptides and oligosaccharides......Page 355
General comments......Page 356
AFFINITY CHROMATOGRAPHY ON IMMOBILIZED LENS CULINARIS AGGLUTININ......Page 357
AFFINITY CHROMATOGRAPHY ON OTHER LECTINS WITH A SPECIFICITY FOR INTERNAL SACCHARIDIC SEQUENCES......Page 359
LECTINS WITH A SPECIFICITY FOR POLYN-ACETYLLACTOSAMINE TYPE GLYCANS......Page 361
LECTINS WITH A SPECIFICITY FOR TERMINAL N-ACETYLLACTOSAMINE SEQUENCES......Page 362
LECTINS WITH A SPECIFICITY FOR SIALYLATED NACETYLLACTOSAMINE SEQUENCES......Page 363
LECTINS RECOGNIZING NON-REDUCING MANNOSE RESIDUES......Page 364
LECTINS RECOGNISING TERMINAL NON-REDUCING N-ACETYLGLUCOSAMINE RESIDUES......Page 366
FUCOSE-BINDING LECTINS......Page 367
Fractionation of O-glycosylpeptides using immobilized lectins......Page 368
CHEMICAL CLEAVAGE OF O- AND N-GLYCOSIDIC LINKAGES......Page 369
ENZYMATIC CLEAVAGE OF N-GLYCOSIDIC LINKAGES......Page 371
PARTITION HPLC OF NEUTRAL AND ACIDIC OLIGOSACCHARIDES ON PRIMARY AMINO-BONDED SILICA......Page 372
Monosialyl oligosaccharides are eluted at a 15mM NaCl concentration, disialyl at 40mM, trisialyl at 50mM and tetrasialyl at 70mM.......Page 374
SEPARATION OF NEUTRAL OLIGOSACCHARIDES......Page 376
SEPARATION OF ACIDIC OLIGOSACCHARIDES......Page 377
References......Page 378
Introduction......Page 387
Fundamentals......Page 388
Resolution and efficiency......Page 391
Ionic surfactants......Page 392
Chiral surfactants......Page 394
Macromolecular surfactants......Page 395
Organic solvents......Page 396
Glucose and urea......Page 397
Cyclodextrins......Page 398
Ion-pairing reagents......Page 399
Online coupling of MEKC with mass spectrometry......Page 401
Introduction......Page 402
Instrumentation......Page 403
Stationary phase......Page 405
Mobile phase......Page 410
Band Spreading in CEC......Page 411
Online coupling of CEC with mass spectrometry......Page 412
References......Page 415
The principle of molecular imprinting......Page 422
Physical properties......Page 424
Cross-linking monomers......Page 425
Porogenic solvents......Page 426
Physical forms of imprinted polymers......Page 427
Applications for molecularly imprinted polymers in separation technology......Page 428
Thin layer chromatography......Page 429
Capillary electrochromatography......Page 430
Solid-phase extraction......Page 431
References......Page 432
Introduction......Page 435
Definitions......Page 436
Modes of operation......Page 437
Thermodynamic equilibrium......Page 438
Ion-exchange chromatography......Page 439
Reverse phase and hydrophobic interaction chromatography......Page 444
Affinity chromatography......Page 445
Other special cases of adsorption chromatography......Page 446
Multicomponent isotherms......Page 447
Dynamics of chromatography......Page 448
Plate model......Page 449
Rate model......Page 450
Gradient-elution chromatography......Page 451
Experimental case studies......Page 454
Concluding remarks......Page 462
Acknowledgments......Page 463
Notations......Page 464
References......Page 466
Dynamics of chromatographic behaviour......Page 469
Discrete plate analysis......Page 470
Parameter estimation: determination of N and the concept of HETP......Page 472
Non-equilibrium and zone spreading......Page 473
Continuous description of chromatography......Page 475
Rate theories......Page 476
General remarks......Page 477
Scale-up......Page 478
Equipment......Page 480
Process hygiene......Page 481
Validation......Page 482
References......Page 483
Validation plan......Page 484
Equipment/hardware and software [3]......Page 485
DESCRIPTION AND JUSTIFICATION OF THE STANDARD CHROMATOGRAPHIC PROCEDURE SCP [4]......Page 486
DESCRIPTION OF COLUMN MAINTENANCE PROCEDURES AND CRITERIA FOR ITS REUSE [5]......Page 487
Process validation studies [2–15]......Page 488
Standard performance qualification studies \0挀漀渀挀甀爀爀攀渀琀⼀瀀爀漀猀瀀攀挀琀椀瘀攀⼀爀攀琀爀漀猀瀀攀挀琀椀瘀攀......Page 489
Prospective scale-down conditions \0瀀爀漀猀瀀攀挀琀椀瘀攀 Numerous scaled-down cycles should be done......Page 490
Viruses clearance validation of chromatographic processes \0㄀㘠ጀ㈀　......Page 491
Changes in chromatography processes [1–2, 21–26]......Page 492
Documentation......Page 493
References......Page 497
Introduction......Page 499
Extracorporeal set ups......Page 501
Liposorber LA 15 \0䬀愀渀攀欀愀......Page 502
DALI \0䘀爀攀猀攀渀椀甀猀......Page 503
Pseudobioadsorption......Page 504
Immusorba \0䄀猀愀栀椀......Page 505
Bioadsorption......Page 506
Immobilized antibodies \0吀栀攀爀愀猀漀爀戀......Page 507
Adequacy of the existing systems for a treatment......Page 509
Usual assessment of biocompatibility......Page 511
Leakage problems......Page 512
Future perspectives......Page 514
References......Page 515