Practical enzymology:
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| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Weinheim
Wiley-VCH
2011
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| Ausgabe: | 2., completely rev. ed. |
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| Beschreibung: | Hier auch später erschienene, unveränderte Nachdrucke |
| Beschreibung: | XVI, 360 S. Ill., graph. Darst. |
| ISBN: | 9783527320769 |
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MARC
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| 100 | 1 | |a Bisswanger, Hans |d 1943- |e Verfasser |0 (DE-588)129060461 |4 aut | |
| 245 | 1 | 0 | |a Practical enzymology |c Hans Bisswanger |
| 250 | |a 2., completely rev. ed. | ||
| 264 | 1 | |a Weinheim |b Wiley-VCH |c 2011 | |
| 300 | |a XVI, 360 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 500 | |a Hier auch später erschienene, unveränderte Nachdrucke | ||
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Datensatz im Suchindex
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IMAGE 1
CONTENTS
PREFACE TO THE SECOND EDITION XIII NOTE TO THE READER XIV ABBREVIATIONS
XV
1 INTRODUCTION 1
STANDARD BOOKS, SERIES, AND DATABASES 3
2 GENERAL ASPECTS OF ENZYME ANALYSIS 5 2.1 BASIC REQUIREMENTS FOR ENZYME
ASSAYS 5 2.2 WHAT MUST BE OBSERVED FOR AN ENZYME ASSAY? 8 2.2.1 ORDER OF
REACTIONS 8
2.2.2 SIGNIFICANCE OF THE REACTION ORDER FOR ENZYME REACTIONS 10 2.2.3
DETERMINATION OF THE VELOCITY OF ENZYME REACTIONS 14 2.2.3.1 ENZYME
UNITS 14 2.2.3.2 PROGRESS CURVES 16 2.2.3.3 DIFFICULTIES IN
DETERMINATION OF INITIAL VELOCITIES 17 2.2.3.4 A SHORT DISCUSSION ON
ERROR 21 2.2.3.5 PREPARATION OF DILUTION SERIES 25 2.2.3.6
CONSIDERATIONS ABOUT STATISTICAL TREATMENTS 27 2.2.4 MICHAELIS-MENTEN
EQUATION 28 2.2.4.1 GENERAL CONSIDERATIONS 28 2.2.4.2 LINEAR
REPRESENTATIONS OF THE MICHAELIS-MENTEN EQUATION 30 2.2.5 ENZYME
INHIBITION 33 2.2.6 MULTISUBSTRATE REACTIONS 39 2.2.7 ESSENTIAL
CONDITIONS FOR ENZYME ASSAYS 41 2.2.7.1 DEPENDENCE ON SOLVENTS AND IONIC
STRENGTH 41 2.2.7.2 PH DEPENDENCY 42 2.2.7.3 ISOELECTRIC POINT 44 2.2.7A
BUFFERS: WHAT MUST BE REGARDED? 44 2.2.7.5 HOW TO PREPARE BUFFERS? 48
2.2.7.6 TEMPERATURE DEPENDENCY 49
BIBLIOGRAFISCHE INFORMATIONEN HTTP://D-NB.INFO/1006150072
DIGITALISIERT DURCH
IMAGE 2
V II CONTENTS
2.2.7.7 WHY ARE ENZYMES UNSTABLE? 53
2.2.7.8 HOW CAN ENZYMES BE STABILIZED? 55 2.2.7.9 HOW TO STORE ENZYMES?
55 2.3 INSTRUMENTAL ASPECTS 57
2.3.1 SPECTROSCOPIC METHODS 57 2.3.1.1 ABSORPTION (UV/VIS) PHOTOMETRY 57
2.3.1.2 CUVETTES 68 2.3.1.3 TURBIDITY MEASUREMENTS 70
2.3.1.4 FLUORESCENCE PHOTOMETRY 71 2.3.1.5 LUMINOMETRY 76 2.3.1.6
POLARIMETRY 77 2.3.2 ELECTROCHEMICAL METHODS 78
2.3.2.1 PH METER AND GLASS ELECTRODES 78 2.3.2.2 PH STAT 79
2.3.2.3 POTENTIOMETRY 79 2.3.2.4 OXYGEN AND CARBON DIOXIDE ELECTRODES 80
2.3.3 RADIOACTIVE LABELING 81 2.3.4 DIVERSE METHODS 81 2.4 THEORY OF
COUPLED ENZYME REACTIONS 83 2.4.1 TWO COUPLED REACTIONS 83 2.4.2 THREE
COUPLED REACTIONS 86 2.5 SUBSTRATE DETERMINATION 86 2.5.1 END POINT
METHOD 87
2.5.2 SUBSTRATE DETERMINATION BY COUPLED ENZYME REACTIONS 88 2.5.3
KINETIC METHOD FOR SUBSTRATE DETERMINATION 89 2.5.4 ENZYMATIC CYCLING 90
3 ENZYME ASSAYS 93
3.1 ENZYME NOMENCLATURE 93
3.2 PRACTICAL CONSIDERATIONS FOR ENZYME ASSAYS 97 3.3 SPECIAL ENZYME
ASSAYS 100 3.3.1 OXIDOREDUCTASES, EC 1 100 3.3.1.1 OPTICAL ASSAY 100
3.3.1.2 FLUORIMETRIC ASSAY 100 3.3.1.3 ALCOHOL DEHYDROGENASE, EC 1.1.1.1
101
A. REDUCTION ASSAY 101 B. OXIDATION ASSAY 102 3.3.1.4 ALCOHOL
DEHYDROGENASE (NADP+), EC 1.1.1.2 103 3.3.1.5 HOMOSERINE DEHYDROGENASE,
EC 1.1.1.3 104 3.3.1.6 SHIKIMATE DEHYDROGENASE, EC 1.1.1.25 105 3.3.1.7
L-LACTATE DEHYDROGENASE, EC 1.1.1.27 106
A. SPECTROPHOTOMETRIC REDUCTION ASSAY 106 B. FLUORIMETRIC REDUCTION
ASSAY 107 C. OXIDATION ASSAY 108 3.3.1.8 MALATE DEHYDROGENASE, EC
1.1.1.37 108
IMAGE 3
CONTENTS VII
3.3.1.9 MALATE DEHYDROGENASE (OXALOACETATE-DECARBOXYLATING) (NAD + ),
EC 1.1.1.38, AND MALATE DEHYDROGENASE (DECARBOXYLATING), EC 1.1.1.39 110
3.3.1.10 MALATE DEHYDROGENASE (OXALOACETATE-DECARBOXYLATING) (NADP+), EC
1.1.1.40 111 3.3.1.11 ISOCITRATE DEHYDROGENASE (NAD+), EC 1.1.1.41 112
3.3.1.12 ISOCITRATE DEHYDROGENASE (NADP+), EC 1.1.1.42 113 3.3.1.13
GLUCOSE-6-PHOSPHATE DEHYDROGENASE, EC 1.1.1.49 114 3.3.1.14 GLUCOSE
OXIDASE, EC 1.1.3.4 115 3.3.1.15 FORMATE DEHYDROGENASE, EC 1.2.1.2 116
3.3.1.16 GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, EC 1.2.1.12 117
A. OXIDATION ASSAY 117 B. REDUCTION ASSAY COUPLED WITH
3-PHOSPHOGLYCERATE KINASE (PGK) 118 3.3.1.17 PYRUVATE DEHYDROGENASE
(ACETYL-TRANSFERRING), EC 1.2.4.1 119
A. FERRICYANIDE AS ELECTRON ACCEPTOR 120 B. DICHLOROPHENOLINDOPHENOL AS
ELECTRON ACCEPTOR 120 3.3.1.18 OXOGLUTARATE DEHYDROGENASE
(SUCCINYL-TRANSFERRING), EC 1.2.4.2 121 3.3.1.19 PYRUVATE FERREDOXIN
OXIDOREDUCTASE, EC 1.2.7.1 123
ASSAY WITH CYTOCHROME C AS ELECTRON ACCEPTOR 123 3.3.1.20 ALANINE
DEHYDROGENASE, EC 1.4.1.1 124 A. OXIDATION OF ALANINE 124 B. REDUCTION
OF PYRUVATE 125 3.3.1.21 GLUTAMATE DEHYDROGENASE, EC 1.4.1.3 125
3.3.1.22 LEUCINE DEHYDROGENASE, EC 1.4.1.9 127 3.3.1.23 L-AMINO ACID
OXIDASE, EC 1.4.3.2 128 3.3.1.24 D-AMINO ACID OXIDASE, EC 1.4.3.3 129
3.3.1.25 MONOAMINE OXIDASE, EC 1.4.3.4 129 3.3.1.26 PRIMARY AMINE
OXIDASE, EC 1.4.3.21 130
A. SPECTROPHOTOMETRIC ASSAY 131 B. POLAROGRAPHIC ASSAY OF O2 UPTAKE WITH
O2 ELECTRODE 131 C. ASSAYS FOR BENZYLAMINE OXIDASE ACTIVITY 132 3.3.1.27
DIAMINE OXIDASE, EC 1.4.3.22 132
3.3.1.28 URATE OXIDASE, EC 1.7.3.3 133 3.3.1.29 DIHYDROLIPOAMIDE
DEHYDROGENASE, EC 1.8.1.4 134 A. OXIDATION OF DIHYDROLIPOAMIDE 135 B.
REDUCTION OF LIPOAMIDE 135
3.3.1.30 GLUTATHIONE DISULFIDE REDUCTASE, EC 1.8.1.7 136 3.3.1.31
CATALASE, EC 1.11.1.6 137 3.3.1.32 PEROXIDASE, EC 1.11.1.7 139 A. ASSAYS
WITH 2,2'-AZINO-BIS-3-ETHYLBENZOTHIAZOLINE-6-SULFONIC ACID
(ABTS) 139 B. ASSAY WITH GUAIACOL 140 C. ASSAY WITH DIANISIDINE 140
3.3.1.33 LUCIFERASE, EC 1.13.12.7 141
IMAGE 4
VIII CONTENTS
3.3.2 TRANSFERASES, EC 2 143
3.3.2.1 DIHYDROLIPOAMIDE ACETYLTRANSFERASE, EC 2.3.1.12 143 A.
SPECTROPHOTOMETRIC ASSAY 143 B. STOPPED ASSAY 145 3.3.2.2 FATTY ACID
SYNTHASE, EC 2.3.1.85 146
3.3.2.3 PHOSPHORYLASE A, EC 2.4.1.1 147 3.3.2.4 ASPARTATE TRANSAMINASE,
EC 2.6.1.1 149 3.3.2.5 ALANINE TRANSAMINASE, EC 2.6.1.2 150 3.3.2.6
TYROSINE TRANSAMINASE, EC 2.6.1.5, TRYPTOPHAN TRANSAMINASE,
EC 2.6.1.27, PHENYLALANINE TRANSAMINASE, EC 2.6.1.58 151 3.3.2.7
HEXOKINASE, EC 2.7.1.1 153 3.3.2.8 PYRUVATE KINASE, EC 2.7.1.40 155
3.3.2.9 ACETATE KINASE, EC 2.7.2.1 156
3.3.2.10 PHOSPHOGLYCERATE KINASE, EC 2.7.2.3 157 3.3.2.11 ASPARTOKINASE,
EC 2.7.2.4 159 3.3.3 HYDROLASES, EC 3 160
3.3.3.1 IIPASE, EC 3.1.1.3 160 A. ASSAY WITH PH-STAT (AUTO TITRATOR) 161
B. FLUORIMETRIC ASSAY 162
3.3.3.2 PHOSPHOLIPASE A 2 , EC 3.1.1.4 162 3.3.3.3
ACETYLCHOLINE-ESTERASE, EC 3.1.1.7 163 3.3.3.4 CHOLINE ESTERASE, EC
3.1.1.8 164 A. PH-STAT ASSAY 165
B. COLORIMETRIC ASSAY 166 3.3.3.5 S-FORMYLGLUTATHIONE HYDROLASE, EC
3.1.2.12 166 3.3.3.6 ALKALINE PHOSPHATASE, EC 3.1.3.1 167 A. MAMMALIAN
ALKALINE PHOSPHATASE 167
B. BACTERIAL ALKALINE PHOSPHATASE 168 3.3.3.7 ACID PHOSPHATASE, EC
3.1.3.2 168 3.3.3.8 RIBONUCLEASE (PANCREATIC), EC 3.1.27.5 169 3.3.3.9
A-AMYLASE, EC 3.2.1.1 170
3.3.3.10 AMYLOGLUCOSIDASE, EC 3.2.1.3 171 A. COUPLED ASSAY WITH HK AND
G6PDH 172 B. PHOTOMETRIC ASSAY WITH 4-NITROPHENYL-D-GLUCOSE 172 C.
FLUORIMETRIC ASSAY WITH 4-METHYLUMBELLIFERYL-A-D-GLUCOSIDE 173 3.3.3.11
CELLULASES, /M,4-GLUCANASE, EC 3.2.1.4, AND ^-GLUCOSIDASE,
EC 3.2.1.21 174 A. ORCINOL ASSAY 174 B. ACTIVITY STAINING 1 75 3.3.3.12
LYSOZYME, EC 3.2.1.17 177 3.3.3.13 SIALIDASE, EC 3.2.1.18 177
A. FLUORIMETRIC ASSAY 178 B. ACTIVITY STAINING 178 3.3.3.14
OR-GLUCOSIDASE, EC 3.2.1.20 179 A. OR-GLUCOSIDASE ASSAY 180
IMAGE 5
CONTENTS IX
B. GLUCOSE DETERMINATION 180
C. ASSAY WITH 4-NITROPHENYLGLUCOPYRANOSIDE 181 3.3.3.15 SS-GALACTOSIDASE,
EC 3.2.1.23 182 3.3.3.16 ^-FRUCTOSIDASE, EC 3.2.1.26 183 3.3.3.17
SS-GLUCURONIDASE EC 3.2.1.31 184
A. FLUORIMETERIC ASSAY 184 3.3.3.18 PROTEASES, EC 3.4, GENERAL ASSAYS
185 A. ANSON ASSAY 185 B. CASEIN-ASSAY 187
C. AZOCASEIN ASSAY 188 D. NINHYDRIN ASSAY 189 3.3.3.19 LEUCINE
AMINOPEPTIDASE, EC 3.4.11.1 190 A. ASSAY WITH LEUCINEAMIDE 191
B. ASSAY WITH LEUCINE-P-NITROANILIDE 391 3.3.3.20 A-CHYMOTRYPSIN, EC
3.4.21.1 192 A. ASSAY WITH SUPHEPA 192
B. ASSAY WITH GLUPHEPA 193 3.3.3.21 PANCREATIC EKSTASE, EC 3.4.21.35
(PREVIOUS EC 3.4.4.7) 194 A. ASSAY WITH
SUCCINYL-ALA-ALA-ALA-P-NITRONILIDE 194
B. ESTERASE ACTIVITY OF ELASTASE 194 3.3.3.22 PEPSIN, EC 3.4.23.1 195
3.3.3.23 TRYPSIN, EC 3.4.21.4 196 3.3.3.24 ASPARAGINASE, EC 3.5.1.1 197
3.3.3.25 GLUTAMINASE, EC 3.5.1.2 198
A. DETERMINATION OF AMMONIA WITH NESSLER'S REAGENT 199 B. PH-STAT ASSAY
199 3.3.3.26 UREASE, EC 3.5.1.5 200 A. PHSTAT ASSAY 201
B. PHOTOMETRIC ASSAY 201 3.3.3.27 ADENOSINETRIPHOSPHATASE, EC 3.6.1.3
202 3.3.4 LYASES, EC 4 203
3.3.4.1 PYRUVATE DECARBOXYLASE, EC 4.1.1.1 203 3.3.4.2 GLUTAMATE
DECARBOXYLASE, EC 4.1.1.15 205 3.3.4.3 ALDOLASE, EC 4.1.2.13 206
3.3.4.4 ANTHRANILATE SYNTHASE, EC 4.1.3.27 207 3.3.4.5 CARBONIC
ANHYDRASE, EC 4.2.1.1 208 A. PH-STAT ASSAY 208 B. ESTERASE ASSAY WITH
4-NITROPHENYLACETATE 209
3.3.4.6 FUMARASE, EC 4.2.1.2 210 3.3.5 ISOMERASES, EC 5 211
3.3.5.1 GLUCOSE/XYLOSE ISOMERASE EC 5.3.1.5 211 A. D-XYLOSE ISOMERASE
ASSAY 211 B. D-XYLOSE ISOMERASE MICROPLATE ASSAY 212 C. D-GLUCOSE
ISOMERASE ASSAY 213
D. D-GLUCOSE ISOMERASE MICROPLATE ASSAY 214
IMAGE 6
X| CONTENTS
3.3.5.2 PHOSPHOGLUCOMUTASE, EC 5.4.2.2 215
3.3.6 IIGASES (SYNTHETASES) EC 6 226 3.3.6.1 TYROSINE-TRNA IIGASE, EC
6.1.1.1 216 A. FLUORIMETRIC ASSAY 216 B. ATP - 32 PP-EXCHANGE 217
3.3.6.2 GLUTAMINE SYNTHETASE EC 6.3.1.2 228 3.3.7 ASSAYS FOR MULTIENZYME
COMPLEXES 220 3.3.7.1 PYRUVATE DEHYDROGENASE COMPLEX (PDHC) 220 A.
OVERALL ACTIVITY OF PDHC BY NAD+ REDUCTION 221
B. OVERALL ACTIVITY OF PDHC BY BY DISMUTATION ASSAY 222 3.3.7.2
A-OXOGLUTARATE DEHYDROGENASE COMPLEX (OGDHC) 224 OVERALL ACTIVITY BY
NAD+ REDUCTION 224 3.3.8 SUBSTRATE DETERMINATION 225
3.3.8.1 DETERMINATION OF NADP(H) BY ENZYMATIC CYCLING 225 3.3.8.2
DETERMINATION OF NAD (H) 227 3.4 ASSAYS FOR ENZYME CHARACTERIZATION 229
3.4.1 PROTEIN DETERMINATION 229 3.4.1.1 BIURET ASSAY 230 3.4.1.2 BCA
ASSAY 232
A. ASSAY FOR SOLUBLE PROTEINS 232 B. MODIFICATION FOR IMMOBILIZED
PROTEINS 233 3.4.1.3 LOWRY ASSAY 234 3.4.1.4 COOMASSIE BINDING ASSAY
(BRADFORD ASSAY) 235 3.4.1.5 ABSORPTION METHOD 236 3.4.1.6 FLUORIMETRIC
ASSAY 238 3.4.1.7 NINHYDRIN ASSAY 239
3.4.1.8 MODIFIED NINHYDRIN ASSAY WITHOUT HYDROLYSIS 240 3.4.1.9 PROTEIN
ASSAY WITH 2-HYDROXY-L-NAPHTHALDEHYDE 242 3.4.2 PHOSPHATE DETERMINATION
243 3.4.3 GLYCOPROTEIN ASSAYS 245
A. DETECTION IN ELECTROPHORESIS GELS 245 B. DETERMINATION OF
PROTEIN-BOUND HEXOSES 245 3.4.4 CROSS-LINKING OF PROTEINS WITH
DIMETHYLSUBERIMIDATE 246 3.4.5 CONCENTRATION OF ENZYME SOLUTIONS 247
3.4.5.1 PRECIPITATION 248
3.4.5.2 ULTRAFILTRATION AND DIALYSIS 251 3.4.5.3 ULTRACENTRIFUGATION 252
3.4.5.4 LYOPHILIZATION 252 3.4.5.5 OTHER CONCENTRATION METHODS 253 3.5
ENZYME IMMUNOASSAYS 254
3.5.1 RADIOIMMUNOASSAYS 254 3.5.2 NONCOMPETITIVE SOLID-PHASE ENZYME
IMMUNOASSAY 256 3.5.3 COMPETITIVE SOLID-PHASE ENZYME IMMUNOASSAY 257
3.5.4 METHODS FOR ENZYME IMMUNOASSAYS AND IMMOBILIZATION
TECHNIQUES 257
IMAGE 7
CONTENTS XI
3.5.4.1 PROTEIN COUPLING TO CYANOGEN BROMIDE-ACTIVATED AGAROSE 257
3.5.4.2 COUPLING OF DIAMINOHEXYL SPACER 259 3.5.4.3 PERIODATE ACTIVATION
OF CELLULOSE 259 3.5.4.4 INTRODUCTION OF THIOL GROUPS INTO PROTEINS
(ANTIBODIES) 260 3.5.4.5 CONJUGATION OF A PROTEIN (ANTIBODY) WITH AN
ENZYME (PEROXIDASE) 262 3.5.4.6 CONJUGATION OF/S-GALACTOSIDASE TO
PROTEINS (ANTIBODIES) BY MBS 262 3.5.4.7 CONJUGATION OF ALKALINE
PHOSPHATASE TO ANTIBODIES BY
GLUTARALDEHYDE 263
4 BINDING MEASUREMENTS 265
4.1 DIFFERENT TYPES OF BINDING 265 4.1.1 GENERAL CONSIDERATIONS 265
4.1.2 HOW TO RECOGNIZE SPECIFIC REVERSIBLE BINDING? 266 4.1.3
EXPERIMENTAL ASPECTS 268 4.2 BINDING MEASUREMENTS BY SIZE DISCRIMINATION
272 4.2.1 EQUILIBRIUM DIALYSIS 271 4.2.1.1 BINDING OF INDOLE TO BOVINE
SERUM ALBUMIN 273 4.2.2 EVALUATION OF BINDING EXPERIMENTS 276 4.2.3
ULTRAFILTRATION 278
4.2.4 GEL FILTRATION 278
4.2.5 ULTRACENTRIFUGATION 280 4.3 SPECTROSCOPIC METHODS 281 4.3.1
DIFFERENCE SPECTROSCOPY 282 4.3.1.1 DIFFERENCE SPECTROSCOPIC TITRATION
OF IIGANDS BINDING TO CATALASE 283 4.3.1.2 EVALUATION OF SPECTROSCOPIC
BINDING CURVES 287 4.3.2 FLUORESCENCE SPECTROSCOPY 289 4.3.2.1 BINDING
OF ANS TO BOVINE SERUM ALBUMIN 290 4.4 OTHER BINDING METHODS 295
4.4.1 RADIOACTIVE LABELING 295 4.4.2 SURFACE PLASMON RESONANCE 295
5 ENZYMES IN TECHNICAL APPLICATIONS 297
5.1 MODES OF ENZYME IMMOBILIZATION 297 5.1.1 ADSORPTION 298
5.1.2 ENTRAPMENT 300
5.1.3 ENCAPSULATION 300
5.1.4 CROSS LINKING 301
5.1.5 COVALENT IMMOBILIZATION TO SOLID SUPPORTS 303 5.1.5.1 SUPPORTS 303
5.1.5.2 SPACER 303
5.2 METHODS FOR ENZYME IMMOBILIZATION 305 5.2.1 MICROENCAPSULATION IN
NYLON BEADS 305 5.2.2 ENTRAPMENT IN POLYACRYLAMIDE 306 5.2.3 COVALENT
IMMOBILIZATION ON GLASS SURFACES 307
5.2.4 COVALENT IMMOBILIZATION ON CONTROLLED-PORE GLASS 309
IMAGE 8
XIII CONTENTS
5.2.5 COVALENT IMMOBILIZATION TO POLYAMIDE 322
5.2.5.1 O-ALKYLATION WITH TRIETHYLOXONIUM TETRAFLUOROBORATE 313 5.2.5.2
IMMOBILIZATION TO AMINO GROUPS AFTER PARTIAL HYDROLYSIS OF POLYAMIDE 325
5.2.5.3 IMMOBILIZATION TO CARBOXYL GROUPS AFTER PARTIAL HYDROLYSIS OF
POLYAMIDE 327
5.2.6 IMMOBILIZATION TO POLYESTER 318 5.2.7 IMMOBILIZATION BY ALKALINE
HYDROLYSIS AND ACTIVATION WITH TOSYLCHLORIDE 320 5.2.8 ALKALINE
HYDROLYSIS AND ACTIVATION BY CARBONYLDIIMIDAZOL 322
5.3 ANALYSIS OF IMMOBILIZED ENZYMES 322 5.3.1 GENERAL PRINCIPLES 322
5.3.2 CONTINUOUS PHOTOMETRIC ASSAYS FOR IMMOBILIZED ENZYMES 324 5.3.3
COFACTORS IN REACTIONS WITH IMMOBILIZED ENZYMES 325
5.4 ENZYME REACTORS 326
5.4.1 BATCH REACTOR (SRIRRED-TANK REACTOR) 327 5.4.2 MEMBRANE REACTOR
327 5.4.3 SOLID BED REACTOR 328 5.4.4 IMMOBILIZED CELLS 329 5.5
BIOSENSORS 329
5.5.1 ENZYME ELECTRODES 329 5.5.2 IMMUNOELECTRODES 333 5.5.3 OTHER
BIOSENSORS 334 5.6 IMMOBILIZED ENZYMES IN THERAPY 335
APPENDIX 337 LIST OF ENZYMES ACCORDING TO THE EC NUMBERS 337
INDEX 353 |
| any_adam_object | 1 |
| author | Bisswanger, Hans 1943- |
| author_GND | (DE-588)129060461 |
| author_facet | Bisswanger, Hans 1943- |
| author_role | aut |
| author_sort | Bisswanger, Hans 1943- |
| author_variant | h b hb |
| building | Verbundindex |
| bvnumber | BV036738831 |
| classification_rvk | VK 8700 WC 4350 WD 5050 |
| classification_tum | CHE 828f |
| ctrlnum | (OCoLC)700331904 (DE-599)DNB1006150072 |
| dewey-full | 572.70721 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 572 - Biochemistry |
| dewey-raw | 572.70721 |
| dewey-search | 572.70721 |
| dewey-sort | 3572.70721 |
| dewey-tens | 570 - Biology |
| discipline | Chemie / Pharmazie Biologie Chemie |
| edition | 2., completely rev. ed. |
| format | Book |
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| genre_facet | Lehrbuch |
| id | DE-604.BV036738831 |
| illustrated | Illustrated |
| indexdate | 2024-07-20T10:49:52Z |
| institution | BVB |
| isbn | 9783527320769 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-020656331 |
| oclc_num | 700331904 |
| open_access_boolean | |
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| physical | XVI, 360 S. Ill., graph. Darst. |
| publishDate | 2011 |
| publishDateSearch | 2011 |
| publishDateSort | 2011 |
| publisher | Wiley-VCH |
| record_format | marc |
| spelling | Bisswanger, Hans 1943- Verfasser (DE-588)129060461 aut Practical enzymology Hans Bisswanger 2., completely rev. ed. Weinheim Wiley-VCH 2011 XVI, 360 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Hier auch später erschienene, unveränderte Nachdrucke Enzym (DE-588)4014988-2 gnd rswk-swf Enzymtechnologie (DE-588)4135962-8 gnd rswk-swf Enzymkinetik (DE-588)4133166-7 gnd rswk-swf (DE-588)4123623-3 Lehrbuch gnd-content Enzymtechnologie (DE-588)4135962-8 s Enzymkinetik (DE-588)4133166-7 s DE-604 Enzym (DE-588)4014988-2 s 1\p DE-604 X:MVB text/html http://deposit.dnb.de/cgi-bin/dokserv?id=3527470&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=020656331&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 | Bisswanger, Hans 1943- Practical enzymology Enzym (DE-588)4014988-2 gnd Enzymtechnologie (DE-588)4135962-8 gnd Enzymkinetik (DE-588)4133166-7 gnd |
| subject_GND | (DE-588)4014988-2 (DE-588)4135962-8 (DE-588)4133166-7 (DE-588)4123623-3 |
| title | Practical enzymology |
| title_auth | Practical enzymology |
| title_exact_search | Practical enzymology |
| title_full | Practical enzymology Hans Bisswanger |
| title_fullStr | Practical enzymology Hans Bisswanger |
| title_full_unstemmed | Practical enzymology Hans Bisswanger |
| title_short | Practical enzymology |
| title_sort | practical enzymology |
| topic | Enzym (DE-588)4014988-2 gnd Enzymtechnologie (DE-588)4135962-8 gnd Enzymkinetik (DE-588)4133166-7 gnd |
| topic_facet | Enzym Enzymtechnologie Enzymkinetik Lehrbuch |
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