Holdings: Practical enzymology

Practical enzymology:

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Bibliographic Details
Main Author:	Bisswanger, Hans 1943- (Author)
Format:	Book
Language:	English
Published:	Weinheim Wiley-VCH 2011
Edition:	2., completely rev. ed.
Subjects:	Enzym Enzymtechnologie Enzymkinetik Lehrbuch
Online Access:	Inhaltstext Inhaltsverzeichnis
Item Description:	Hier auch später erschienene, unveränderte Nachdrucke
Physical Description:	XVI, 360 S. Ill., graph. Darst.
ISBN:	9783527320769

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adam_text	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-
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author_facet	Bisswanger, Hans 1943-
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author_sort	Bisswanger, Hans 1943-
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discipline	Chemie / Pharmazie Biologie Chemie
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language	English
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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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work_keys_str_mv	AT bisswangerhans practicalenzymology

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