Fundamentals of enzyme kinetics:
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Weinheim
Wiley-Blackwell
2012
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| Ausgabe: | 4., completly revised and greatly enlarged ed. |
| Schlagworte: | |
| Online-Zugang: | Inhaltstext Inhaltsverzeichnis |
| Beschreibung: | XVIII, 498 S. Ill., graph. Darst. |
| ISBN: | 9783527330744 3527330747 |
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Datensatz im Suchindex
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IMAGE 1
CONTENTS
BASIC PRINCIPLES OF CHEMICAL KINETICS 1
1.1 SYMBOLS, TERMINOLOGY AND ABBREVIATIONS 1
1.2 ORDER OF A REACTION 3
1.2.1 ORDER AND MOLECULARITY 3
1.2.2 FIRST-ORDER KINETICS 4
1.2.3 SECOND-ORDER KINETICS 5
1.2.4 THIRD-ORDER KINETICS 7
1.2.5 ZERO-ORDER KINETICS 8
1.2.6 DETERMINATION OF THE ORDER OF A REACTION 8
1.3 DIMENSIONS OF RATE CONSTANTS 9
1.4 REVERSIBLE REACTIONS 10
1.5 DETERMINATION OF FIRST-ORDER RATE CONSTANTS 11
1.6 THE STEADY STATE 13
1.7 CATALYSIS 14
1.8 THE INFLUENCE OF TEMPERATURE AND PRESSURE ON RATE CONSTANTS 15
1.8.1 THE ARRHENIUS EQUATION 15
1.8.2 ELEMENTARY COLLISION THEORY 17
1.8.3 TRANSITION-STATE THEORY 18
1.8.4 EFFECTS OF HYDROSTATIC PRESSURE 21
CHAPTER SUMMARY 22
PROBLEMS 23
INTRODUCTION TO ENZYME KINETICS 25
2.1 THE IDEA OF AN ENZYME-SUBSTRATE COMPLEX 25
2.2 THE MICHAELIS-MENTEN EQUATION 28
2.3 THE STEADY STATE OF AN ENZYME-CATALYZED REACTION 32
2.3.1 THE BRIGGS-HALDANE TREATMENT 32
2.3.2 PARAMETERS OF THE MICHAELIS-MENTEN EQUATION 33
2.3.3 UNITS OF ENZYME ACTIVITY 34
2.3.4 THE CURVE DEFINED BY THE MICHAELIS-MENTEN EQUATION 35
BIBLIOGRAFISCHE INFORMATIONEN HTTP://D-NB.INFO/1015578411
DIGITALISIERT DURCH
IMAGE 2
VI CONTENTS
2.3.5 MUTUAL DEPLETION KINETICS 37
2.3.6 WAYS OF WRITING THE MICHAELIS-MENTEN EQUATION 37
2.4 SPECIFICITY 38
2.4.1 THE FUNDAMENTAL PROPERTY OF ENZYMES 38
2.4.2 DISCRIMINATION BETWEEN MIXED SUBSTRATES 39
2.4.3 COMPARING DIFFERENT CATALYSTS 42
2.5 VALIDITY OF THE STEADY-STATE ASSUMPTION 43
2.6 GRAPHS OF THE MICHAELIS-MENTEN EQUATION 45
2.6.1 PLOTTING V AGAINST A 45
2.6.2 THE DOUBLE-RECIPROCAL PLOT 47
2.6.3 THE PLOT OIA/V AGAINST A 48
2.6.4 THE PLOT OF V AGAINST V/A 49
2.6.5 ORIGINS OF THE PLOTS 51
2.6.6 THE DIRECT LINEAR PLOT 51
2.7 THE REVERSIBLE MICHAELIS-MENTEN MECHANISM 54
2.7.1 THE REVERSIBLE RATE EQUATION 54
2.7.2 THE HALDANE RELATIONSHIP 58
2.7.3 "ONE-WAY ENZYMES" 59
2.8 PRODUCT INHIBITION 61
2.9 INTEGRATION OF ENZYME RATE EQUATIONS 63
2.9.1 MICHAELIS-MENTEN EQUATION WITHOUT PRODUCT INHIBITION 63 2.9.2
EFFECT OF PRODUCT INHIBITION ON PROGRESS CURVES 65
2.9.3 OTHER PROBLEMS WITH TIME COURSES 66
2.9.4 CHARACTERIZING MUTANT ENZYMES 67
2.9.5 ACCURATE ESTIMATION OF INITIAL RATES 67
2.9.6 TIME COURSES FOR OTHER MECHANISMS 71
CHAPTER SUMMARY 72
PROBLEMS 73
3 "ALTERNATIVE" ENZYMES 77
3.1 INTRODUCTION 77
3.2 ARTIFICIAL ENZYMES 78
3.3 SITE-DIRECTED MUTAGENESIS 80
3.4 CHEMICAL MIMICS OF ENZYME CATALYSIS 81
3.5 CATALYTIC RNA 81
3.6 CATALYTIC ANTIBODIES 83
CHAPTER SUMMARY 84
PROBLEMS 84
4 PRACTICAL ASPECTS OF KINETICS 85
4.1 ENZYME ASSAYS 85
4.1.1 DISCONTINUOUS AND CONTINUOUS ASSAYS 85
4.1.2 ESTIMATING THE INITIAL RATE 86
4.1.3 INCREASING THE STRAIGHTNESS OF THE PROGRESS CURVE 88
4.1.4 COUPLED ASSAYS 89
IMAGE 3
CONTENTS VII
4.2 DETECTING ENZYME INACTIVATION 93
4.3 EXPERIMENTAL DESIGN 95
4.3.1 CHOICE OF SUBSTRATE CONCENTRATIONS 95
4.3.2 CHOICE OF PH, TEMPERATURE AND OTHER CONDITIONS 98
4.3.3 USE OF REPLICATE OBSERVATIONS 99
4.4 TREATMENT OF IONIC EQUILIBRIA 102
CHAPTER SUMMARY 105
PROBLEMS 106
5 DERIVING STEADY-STATE RATE EQUATIONS 107
5.1 INTRODUCTION 107
5.2 THE PRINCIPLE OF THE KING-AIRMAN METHOD 108
5.3 THE METHOD OF KING AND ALTMAN 113
5.4 THE METHOD OF WONG AND HANES 116
5.5 MODIFICATIONS TO THE KING-ALTMAN METHOD 117
5.6 REACTIONS CONTAINING STEPS AT EQUILIBRIUM 119
5.7 ANALYZING MECHANISMS BY INSPECTION 122
5.7.1 TOPOLOGICAL REASONING 122
5.7.2 MECHANISMS WITH ALTERNATIVE ROUTES 123
5.7.3 DEAD-END STEPS 124
5.7.4 UNDETECTABILITY OF SOME ISOMERIZATION STEPS 125
5.8 A SIMPLER METHOD FOR IRREVERSIBLE REACTIONS 126
5.9 DERIVATION OF RATE EQUATIONS BY COMPUTER 128
CHAPTER SUMMARY 131
PROBLEMS 132
6 REVERSIBLE INHIBITION AND ACTIVATION 133
6.1 INTRODUCTION 133
6.2 LINEAR INHIBITION 134
6.2.1 COMPETITIVE INHIBITION 134
6.2.2 MIXED INHIBITION 136
6.2.3 UNCOMPETITIVE INHIBITION 139
6.2.4 SUMMARY OF LINEAR INHIBITION TYPES 140
6.3 PLOTTING INHIBITION RESULTS 140
6.3.1 SIMPLE PLOTS 140
6.3.2 COMBINATION PLOTS 144
6.4 MULTIPLE INHIBITORS 145
6.5 RELATIONSHIP BETWEEN INHIBITION CONSTANTS AND THE CONCENTRATION FOR
50% INHIBITION 147
6.6 INHIBITION BY A COMPETING SUBSTRATE 149
6.6.1 COMPETITION BETWEEN SUBSTRATES 149
6.6.2 TESTING IF TWO REACTIONS OCCUR AT THE SAME SITE 150
6.7 ENZYME ACTIVATION 152
6.7.1 MISCELLANEOUS USES OF THE TERM ACTIVATION 152
6.7.2 ESSENTIAL ACTIVATION 153
IMAGE 4
VIII CONTENTS
6.7.3 MIXED ACTIVATION 155
6.7.4 HYPERBOLIC ACTIVATION AND INHIBITION 155
6.8 DESIGN OF INHIBITION EXPERIMENTS 157
6.9 INHIBITORY EFFECTS OF SUBSTRATES 159
6.9.1 NONPRODUCTIVE BINDING 159
6.9.2 SUBSTRATE INHIBITION 162
CHAPTER SUMMARY 164
PROBLEMS 165
7 TIGHT-BINDING AND IRREVERSIBLE INHIBITORS 169
7.1 TIGHT-BINDING INHIBITORS 169
7.2 IRREVERSIBLE INHIBITORS 172
7.2.1 NONSPECIFIC IRREVERSIBLE INHIBITION 172
7.2.2 SPECIFIC IRREVERSIBLE INHIBITION 173
7.3 SUBSTRATE PROTECTION EXPERIMENTS 174
7.4 MECHANISM-BASED INACTIVATION 175
7.5 CHEMICAL MODIFICATION AS A MEANS OF IDENTIFYING ESSENTIAL GROUPS 179
7.5.1 KINETIC ANALYSIS OF CHEMICAL MODIFICATION 180
7.5.2 REMAINING ACTIVITY AS A FUNCTION OF DEGREE OF MODIFICATION 181 7.6
INHIBITION AS THE BASIS OF DRUG DESIGN 183
7.7 DELIVERING A DRUG TO ITS TARGET 186
CHAPTER SUMMARY 187
PROBLEMS 188
8 REACTIONS OF MORE THAN ONE SUBSTRATE 189
8.1 INTRODUCTION 189
8.2 CLASSIFICATION OF MECHANISMS 190
8.2.1 TERNARY-COMPLEX MECHANISMS 190
8.2.2 SUBSTITUTED-ENZYME MECHANISMS 193
8.2.3 COMPARISON BETWEEN CHEMICAL AND KINETIC CLASSIFICATIONS 195 8.2.4
SCHEMATIC REPRESENTATION OF MECHANISMS 197
8.3 RATE EQUATIONS 198
8.3.1 COMPULSORY-ORDER TERNARY-COMPLEX MECHANISM 198
8.3.2 RANDOM-ORDER TERNARY-COMPLEX MECHANISM 200
8.3.3 SUBSTITUTED-ENZYME MECHANISM 202
8.3.4 HALDANE RELATIONSHIPS 202
8.3.5 CALCULATION OF RATE CONSTANTS FROM KINETIC PARAMETERS 203 8.4
INITIAL-RATE MEASUREMENTS IN THE ABSENCE OF PRODUCTS 204
8.4.1 MEANINGS OF THE PARAMETERS 204
8.4.2 APPARENT MICHAELIS-MENTEN PARAMETERS 207
8.4.3 PRIMARY PLOTS FOR TERNARY-COMPLEX MECHANISMS 208
8.4.4 SECONDARY PLOTS 209
8.4.5 PLOTS FOR THE SUBSTITUTED-ENZYME MECHANISM 210
8.5 SUBSTRATE INHIBITION 211
8.5.1 WHY SUBSTRATE INHIBITION OCCURS 211
IMAGE 5
CONTENTS IX
8.5.2 COMPULSORY-ORDER TERNARY-COMPLEX MECHANISM 211
8.5.3 RANDOM-ORDER TERNARY-COMPLEX MECHANISM 212
8.5.4 SUBSTITUTED-ENZYME MECHANISM 212
8.5.5 DIAGNOSTIC VALUE OF SUBSTRATE INHIBITION 213
8.6 PRODUCT INHIBITION 213
8.7 DESIGN OF EXPERIMENTS 217
8.8 REACTIONS WITH THREE OR MORE SUBSTRATES 218
8.8.1 QUATERNARY-COMPLEX MECHANISMS 219
8.8.2 SUBSTITUTED-ENZYME MECHANISMS 219
8.8.3 HYBRID MECHANISMS 220
8.8.4 CLASSIFICATION OF THREE-SUBSTRATE MECHANISMS 221
CHAPTER SUMMARY 223
PROBLEMS 224
9 USE OF ISOTOPES FOR STUDYING ENZYME MECHANISMS 227
9.1 ISOTOPE EXCHANGE AND ISOTOPE EFFECTS 227
9.2 PRINCIPLES OF ISOTOPE EXCHANGE 228
9.3 ISOTOPE EXCHANGE AT EQUILIBRIUM 231
9.4 ISOTOPE EXCHANGE IN SUBSTITUTED-ENZYME MECHANISMS 233
9.5 NONEQUILIBRIUM ISOTOPE EXCHANGE 234
9.5.1 CHEMIFLUX RATIOS 234
9.5.2 ISOMERASE KINETICS 238
9.5.3 TRACER PERTURBATION 240
9.6 THEORY OF KINETIC ISOTOPE EFFECTS 242
9.6.1 PRIMARY ISOTOPE EFFECTS 242
9.6.2 SECONDARY ISOTOPE EFFECTS 245
9.6.3 EQUILIBRIUM ISOTOPE EFFECTS 246
9.7 PRIMARY ISOTOPE EFFECTS IN ENZYME KINETICS 246
9.8 SOLVENT ISOTOPE EFFECTS 248
CHAPTER SUMMARY 251
PROBLEMS 252
10 EFFECT OF PH ON ENZYME ACTIVITY 253
10.1 ENZYMES AND PH 253
10.2 ACID-BASE PROPERTIES OF PROTEINS 255
10.3 IONIZATION OF A DIBASIC ACID 257
10.3.1 EXPRESSION IN TERMS OF GROUP DISSOCIATION CONSTANTS 257 10.3.2
MOLECULAR DISSOCIATION CONSTANTS 259
10.3.3 BELL-SHAPED CURVES 260
10.4 EFFECT OF PH ON ENZYME KINETIC CONSTANTS 261
10.4.1 UNDERLYING ASSUMPTIONS 261
10.4.2 PH DEPENDENCE OF V AND V/K M 262
10.4.3 PH-INDEPENDENT PARAMETERS AND THEIR RELATIONSHIP TO "APPARENT"
PARAMETERS 264
10.4.4 PH DEPENDENCE OF K M 265
IMAGE 6
CONTENTS
10.4.5 EXPERIMENTAL DESIGN 266
10.5 IONIZATION OF THE SUBSTRATE 268
10.6 "CROSSED-OVER" IONIZATION 268
10.7 MORE COMPLICATED PH EFFECTS 269
CHAPTER SUMMARY 269
PROBLEMS 270
11 TEMPERATURE EFFECTS ON ENZYME ACTIVITY 273
11.1 TEMPERATURE DENATURATION 273
11.2 IRREVERSIBLE DENATURATION 275
11.3 TEMPERATURE OPTIMUM 275
11.4 APPLICATION OF THE ARRHENIUS EQUATION TO ENZYMES 276
11.5 ENTROPY-ENTHALPY COMPENSATION 278
CHAPTER SUMMARY 279
PROBLEMS 280
12 REGULATION OF ENZYME ACTIVITY 281
12.1 FUNCTION OF COOPERATIVE AND ALLOSTERIC INTERACTIONS 281
12.1.1 FUTILE CYCLES 281
12.1.2 INADEQUACY OF MICHAELIS-MENTEN KINETICS FOR REGULATION 283 12.1.3
COOPERATIVITY 284
12.1.4 ALLOSTERIC INTERACTIONS 285
12.2 THE DEVELOPMENT OF MODELS FOR COOPERATIVITY 286
12.2.1 THE HILL EQUATION 286
12.2.2 SPECIFICITY OF NON-MICHAELIS-MENTEN ENZYMES 288
12.2.3 AN ALTERNATIVE INDEX OF COOPERATIVITY 289
12.2.4 ASSUMPTION OF EQUILIBRIUM BINDING IN COOPERATIVE KINETICS 290
12.2.5 THE ADAIR EQUATION 291
12.2.6 MECHANISTIC AND OPERATIONAL DEFINITIONS OF COOPERATIVITY 295 12.3
ANALYSIS OF BINDING EXPERIMENTS 297
12.3.1 EQUILIBRIUM DIALYSIS 297
12.3.2 THE SCATCHARD PLOT 298
12.4 INDUCED FIT 302
12.4.1 ENZYME SPECIFICITY 302
12.4.2 INDUCED FIT TODAY 304
12.5 THE SYMMETRY MODEL OF MONOD, WYMAN AND CHANGEUX 304
12.5.1 BASIC POSTULATES OF THE SYMMETRY MODEL 304
12.5.2 ALGEBRAIC ANALYSIS 306
12.5.3 PROPERTIES IMPLIED BY THE BINDING EQUATION 307
12.5.4 HETEROTROPIC EFFECTS 310
12.6 COMPARISON BETWEEN THE PRINCIPAL MODELS OF COOPERATIVITY 312 12.7
THE SEQUENTIAL MODEL OF KOSHLAND, NEMETHY AND FILMER 313
12.7.1 POSTULATES 313
12.7.2 ALGEBRAIC ANALYSIS 315
12.7.3 PROPERTIES IMPLIED BY THE BINDING EQUATION 318
IMAGE 7
CONTENTS XI
12.8 ASSOCIATION-DISSOCIATION MODELS OF COOPERATIVITY 319
12.9 KINETIC COOPERATIVITY 320
CHAPTER SUMMARY 323
PROBLEMS 324
13 MULTIENZYME SYSTEMS 327
13.1 ENZYMES IN THEIR PHYSIOLOGICAL CONTEXT 327
13.1.1 ENZYMES AS COMPONENTS OF SYSTEMS 327
13.1.2 MOIETY CONSERVATION 328
13.1.3 ENZYMES IN PERMEABILIZED CELLS 329
13.2 METABOLIC CONTROL ANALYSIS 330
13.3 ELASTICITIES 332
13.3.1 DEFINITION OF ELASTICITY 332
13.3.2 COMMON PROPERTIES OF ELASTICITIES 336
13.3.3 ENZYME KINETICS VIEWED FROM CONTROL ANALYSIS 337
13.3.4 RATES AND CONCENTRATIONS AS EFFECTS, NOT CAUSES 338
13.4 CONTROL COEFFICIENTS 341
13.4.1 DEFINITIONS 341
13.4.2 THE PERTURBING PARAMETER 344
13.5 PROPERTIES OF CONTROL COEFFICIENTS 344
13.5.1 SUMMATION RELATIONSHIPS 344
13.5.2 IMPLICATIONS FOR LARGE PERTURBATIONS 347
13.5.3 CONSTRAINED ENZYME CONCENTRATIONS 349
13.6 RELATIONSHIPS BETWEEN ELASTICITIES AND CONTROL COEFFICIENTS 350
13.6.1 CONNECTIVITY PROPERTIES 350
13.6.2 CONTROL COEFFICIENTS IN A THREE-STEP PATHWAY 352
13.6.3 EXPRESSION OF SUMMATION AND CONNECTIVITY RELATIONSHIPS IN MATRIX
FORM 354
13.6.4 CONNECTIVITY RELATIONSHIP FOR A METABOLITE NOT INVOLVED IN
FEEDBACK 355 13.6.5 THE FLUX CONTROL COEFFICIENT OF AN ENZYME FOR THE
FLUX THROUGH ITS OWN REACTION 355
13.7 RESPONSE COEFFICIENTS: THE PARTITIONED RESPONSE 356
13.8 CONTROL AND REGULATION 359
13.9 MECHANISMS OF REGULATION 362
13.9.1 METABOLITE CHANNELING 362
13.9.2 INTERCONVERTIBLE ENZYME CASCADES 365
13.9.3 THE METABOLIC ROLE OF ADENYLATE KINASE 366
13.10 COMPUTER MODELING OF METABOLIC SYSTEMS 368
13.10.1 GENERAL CONSIDERATIONS 368
13.10.2 PROGRAMS FOR MODELING 368
13.10.3 THE REVERSIBLE HILL EQUATION 370
13.10.4 EXAMPLES OF COMPUTER MODELS OF METABOLISM 372
13.11 BIOTECHNOLOGY AND DRUG DISCOVERY 373
CHAPTER SUMMARY 377
PROBLEMS 379
IMAGE 8
XII CONTENTS
14 FAST REACTIONS 381
14.1 LIMITATIONS OF STEADY-STATE MEASUREMENTS 381
14.1.1 THE TRANSIENT STATE 381
14.1.2 THE RELAXATION TIME 382
14.1.3 "SLOW" AND "FAST" STEPS IN MECHANISMS 383
14.1.4 AMBIGUITIES IN THE STEADY-STATE ANALYSIS OF SYSTEMS WITH
INTERMEDIATE ISOMERIZATION 385
14.1.5 ILL-CONDITIONING 386
14.2 PRODUCT RELEASE BEFORE COMPLETION OF THE CATALYTIC CYCLE 388
14.2.1 "BURST" KINETICS 388
14.2.2 ACTIVE SITE TITRATION 390
14.3 EXPERIMENTAL TECHNIQUES 391
14.3.1 CLASSES OF METHOD 391
14.3.2 CONTINUOUS FLOW 392
14.3.3 STOPPED FLOW 393
14.3.4 QUENCHED FLOW 394
14.3.5 FLASH PHOTOLYSIS 396
14.3.6 MAGNETIC RESONANCE METHODS 398
14.3.7 RELAXATION METHODS 399
14.4 TRANSIENT-STATE KINETICS 400
14.4.1 SYSTEMS FAR FROM EQUILIBRIUM 400
14.4.2 SIMPLIFICATION OF COMPLICATED MECHANISMS 405
14.4.3 SYSTEMS CLOSE TO EQUILIBRIUM 408
CHAPTER SUMMARY 410
PROBLEMS 411
15 ESTIMATION OF KINETIC CONSTANTS 413
15.1 DATA ANALYSIS IN AN AGE OF KITS 413
15.2 THE EFFECT OF EXPERIMENTAL ERROR ON KINETIC ANALYSIS 414
15.3 LEAST-SQUARES FIT TO THE MICHAELIS-MENTEN EQUATION 418
15.3.1 INCLUDING ERROR IN THE EQUATION 418
15.3.2 ESTIMATION OF THE MICHAELIS-MENTEN PARAMETERS 420
15.3.3 CORRESPONDING RESULTS FOR A UNIFORM STANDARD DEVIATION IN THE
RATES 422
15.3.4 ESTIMATING WEIGHTS FROM REPLICATE OBSERVATIONS 424
15.4 STATISTICAL ASPECTS OF THE DIRECT LINEAR PLOT 425
15.4.1 COMPARISON BETWEEN CLASSICAL AND DISTRIBUTION-FREE STATISTICS 425
15.4.2 APPLICATION TO THE DIRECT LINEAR PLOT 427
15.4.3 LACK OF NEED FOR WEIGHTING 429
15.4.4 INSENSITIVITY TO OUTLIERS 429
15.4.5 HANDLING OF NEGATIVE PARAMETER ESTIMATES 430
15.5 PRECISION OF ESTIMATED KINETIC PARAMETERS 432
15.5.1 EXPERIMENTAL VARIANCE 432
15.5.2 VARIANCES OF THE MICHAELIS-MENTEN PARAMETERS 433
IMAGE 9
CONTENTS XIII
15.5.3 STANDARD ERRORS 434
15.5.4 K M AS THE LEAST PRECISE MICHAELIS-MENTEN PARAMETER 436
15.6 GENERALIZING THE RESULTS TO MORE THAN TWO PARAMETERS 438
15.6.1 THE GENERAL LINEAR MODEL 438
15.6.2 COMPARING MODELS 439
15.7 USING EXISTING PROGRAMS FOR ANALYZING KINETIC DATA 440
15.8 RESIDUAL PLOTS AND THEIR USES 443
CHAPTER SUMMARY 448
PROBLEMS 449
STANDARDS FOR REPORTING ENZYMOLOGY DATA 451
SOLUTIONS AND NOTES TO PROBLEMS 459
INDEX 473 |
| any_adam_object | 1 |
| author | Cornish-Bowden, Athel 1943- |
| author_GND | (DE-588)1047958619 |
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| author_sort | Cornish-Bowden, Athel 1943- |
| author_variant | a c b acb |
| building | Verbundindex |
| bvnumber | BV039892925 |
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| ctrlnum | (OCoLC)780119459 (DE-599)DNB1015578411 |
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| dewey-ones | 572 - Biochemistry |
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| dewey-search | 572.744 |
| dewey-sort | 3572.744 |
| dewey-tens | 570 - Biology |
| discipline | Chemie / Pharmazie Biologie Chemie |
| edition | 4., completly revised and greatly enlarged ed. |
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| id | DE-604.BV039892925 |
| illustrated | Illustrated |
| indexdate | 2024-07-21T00:24:45Z |
| institution | BVB |
| isbn | 9783527330744 3527330747 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-024751925 |
| oclc_num | 780119459 |
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| physical | XVIII, 498 S. Ill., graph. Darst. |
| publishDate | 2012 |
| publishDateSearch | 2012 |
| publishDateSort | 2012 |
| publisher | Wiley-Blackwell |
| record_format | marc |
| spelling | Cornish-Bowden, Athel 1943- Verfasser (DE-588)1047958619 aut Fundamentals of enzyme kinetics Athel Cornish-Bowden 4., completly revised and greatly enlarged ed. Weinheim Wiley-Blackwell 2012 XVIII, 498 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Enzym (DE-588)4014988-2 gnd rswk-swf Reaktionskinetik (DE-588)4048655-2 gnd rswk-swf Enzymkinetik (DE-588)4133166-7 gnd rswk-swf Enzymkinetik (DE-588)4133166-7 s DE-604 Enzym (DE-588)4014988-2 s Reaktionskinetik (DE-588)4048655-2 s 1\p DE-604 X:MVB text/html http://deposit.dnb.de/cgi-bin/dokserv?id=3887215&prov=M&dok_var=1&dok_ext=htm Inhaltstext DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=024751925&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis 1\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk |
| spellingShingle | Cornish-Bowden, Athel 1943- Fundamentals of enzyme kinetics Enzym (DE-588)4014988-2 gnd Reaktionskinetik (DE-588)4048655-2 gnd Enzymkinetik (DE-588)4133166-7 gnd |
| subject_GND | (DE-588)4014988-2 (DE-588)4048655-2 (DE-588)4133166-7 |
| title | Fundamentals of enzyme kinetics |
| title_auth | Fundamentals of enzyme kinetics |
| title_exact_search | Fundamentals of enzyme kinetics |
| title_full | Fundamentals of enzyme kinetics Athel Cornish-Bowden |
| title_fullStr | Fundamentals of enzyme kinetics Athel Cornish-Bowden |
| title_full_unstemmed | Fundamentals of enzyme kinetics Athel Cornish-Bowden |
| title_short | Fundamentals of enzyme kinetics |
| title_sort | fundamentals of enzyme kinetics |
| topic | Enzym (DE-588)4014988-2 gnd Reaktionskinetik (DE-588)4048655-2 gnd Enzymkinetik (DE-588)4133166-7 gnd |
| topic_facet | Enzym Reaktionskinetik Enzymkinetik |
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| work_keys_str_mv | AT cornishbowdenathel fundamentalsofenzymekinetics |