Enzyme kinetics: principles and methods
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Format: | Buch |
Sprache: | English German |
Veröffentlicht: |
Weinheim
WILEY-VCH
2008
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Ausgabe: | 2., rev. and updated ed. |
Schlagworte: | |
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Beschreibung: | Früher mit der Nummer 9783527303434 |
Beschreibung: | XVIII, 301 S. graph. Darst. 240 mm x 170 mm |
ISBN: | 9783527319572 3527319573 |
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084 | |a 570 |2 sdnb | ||
100 | 1 | |a Bisswanger, Hans |d 1943- |e Verfasser |0 (DE-588)129060461 |4 aut | |
245 | 1 | 0 | |a Enzyme kinetics |b principles and methods |c Hans Bisswanger |
250 | |a 2., rev. and updated ed. | ||
264 | 1 | |a Weinheim |b WILEY-VCH |c 2008 | |
300 | |a XVIII, 301 S. |b graph. Darst. |c 240 mm x 170 mm | ||
336 | |b txt |2 rdacontent | ||
337 | |b n |2 rdamedia | ||
338 | |b nc |2 rdacarrier | ||
500 | |a Früher mit der Nummer 9783527303434 | ||
650 | 4 | |a Cinétique enzymatique | |
650 | 4 | |a Cinétique enzymatique - Méthodologie | |
650 | 4 | |a Enzyme kinetics | |
650 | 4 | |a Enzymes |x metabolism | |
650 | 4 | |a Kinetics | |
650 | 0 | 7 | |a Methode |0 (DE-588)4038971-6 |2 gnd |9 rswk-swf |
650 | 0 | 7 | |a Enzymkinetik |0 (DE-588)4133166-7 |2 gnd |9 rswk-swf |
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Datensatz im Suchindex
_version_ | 1805089985514176512 |
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adam_text |
XI
Contents
Preface
to the Second English Edition
VII
Prefece
to the First English Edition IX
Symbols and Abbreviations
XVII
Introduction and Definitions
1
References
4
1
Multiple Equilibria
7
1.1
Diffusion
8
1.2
Interaction between Macromolecules and Ligands
12
1.2.1
Binding Constants
12
1.2.2
Macromolecules with One Binding Site
13
1.3
Macromolecules with Identical Independent Binding Sites
14
1.3.1
General Binding Equation
14
1.3.2
Graphic Representations of the Binding Equation
20
1.3.2.1
Direct and Linear Diagrams
20
1.3.2.2
Analysis of Binding Data from
Spectroscopie
Titrations 22
1.3.3
Binding of Different Ligands, Competition
25
1.3.4
Non-competitive Binding
27
1.4
Macromolecules with Non-identical, Independent Binding Sites
29
1.5
Macromolecules with Identical, Interacting Binding Sites,
Cooperativity
32
1.5.1
The Hill Equation
32
1.5.2
The Adair Equation
34
1.5.3
The Pauling Model
37
1.5.4
Allosteric Enzymes
38
1.5.5
The Symmetry or Concerted Model
39
1.5.6
The Sequential Model and Negative Cooperativity
44
1.5.7
Analysis of Cooperativity
48
1.5.8
Physiological Aspects of Cooperativity
50
1.5.9
Examples of Allosteric Enzymes
52
Enzyme Kinetics. Principles and Methods.
2nå
Ш.
Hans Bisswanger
Copyright
© 2008
WILEY-VCH
Verlag
GmbH
&
Co. KGaA, Weinheim
ISBN:
978-3-527-31957-2
XII Contents
1.5.9.1
Hemoglobin
52
1.5.9.2
Aspartate
Transcarbamoylase
53
1.5.9.3 Aspartokinase 54
1.5.9.4 Phosphofractokinase 55
1.5.9.5 Allosteric Regulation
of the
Glycogen
Metabolism
55
1.5.9.6 Membrane
Bound Enzymes and Receptors
55
1.6
Non-identical, Interacting Binding Sites
56
References
57
2
Enzyme Kinetics
59
2.1
Reaction Order
59
2.1.1
First Order Reactions
60
2.1.2
Second Order Reactions
61
2.1.3
Zero Order Reactions
62
2.2
Steady-State Kinetics and the Michaelis-Menten Equation
63
2.2.1
Derivation of the Michaelis-Menten Equation
63
2.3
Analysis of Enzyme Kinetic Data
66
2.3.1
Graphical Representations of the Michaelis-Menten Equation
66
2.3.1.1
Direct and Semi-logarithmic Representations
66
2.3.1.2
Direct Linear Plots
73
2.3.1.3
Linearization Methods
75
2.3.2
Analysis of Progress Curves
77
2.3.2.1
Integrated Michaelis-Menten Equation
78
2.3.2.2
Determination of Reaction Rates
80
2.3.2.3
Graphic Methods for Rate Determination
82
2.3.2.4
Graphic Determination of True Initial Rates
84
2.4
Reversible Enzyme Reactions
85
2.4.1
Rate Equation for Reversible Enzyme Reactions
85
2.4.2
The Haldane Relationship
87
2.4.3
Product Inhibition
88
2.5
Enzyme Inhibition
91
2.5.1
Unspecific Enzyme Inhibition
91
2.5.2
Irreversible Enzyme Inhibition
92
2.5.2.1
General Features of Irreversible Enzyme Inhibition
92
2.5.2.2
Suicide Substrates
93
2.5.2.3
Transition State Analogs
95
2.5.2.4
Analysis of Irreversible Inhibitions
96
2.5.3
Reversible Enzyme Inhibition
98
2.5.3.1
General Rate Equation
98
2.5.3.2
Non-Competitive Inhibition and Graphic Representation
of Inhibition Data
101
2.5.3.3
Competitive Inhibition
107
2.5.3.4
Uncompetitive Inhibition 111
2.5.3.5
Partially Non-competitive Inhibition
113
Contents XIII
2.5.3.6
Partially Uncompetitive Inhibition
115
2.5.3.7
Partially Competitive Inhibition
117
2.5.3.8
Noncompetitive
and Uncompetitive Product Inhibition
119
2.5.3.9
Substrate Inhibition
120
2.5.4
Enzyme Reactions with Two Competing Substrates
121
2.5.5
Different Enzymes Catalyzing the Same Reaction
123
2.6
Multi-substrate Reactions
124
2.6.1
Nomenclature
124
2.
ii.
2
Random Mechanism
126
2.6.3
Ordered Mechanism
131
2.6.4
Ping-pong Mechanism
132
2.6.5
Product Inhibition in Multi-substrate Reactions
135
2.6.6
Haldane Relationships in Multi-substrate Reactions
135
2.6.7
Mechanisms with more than Two Substrates
136
2.6.8
Other Nomenclatures for Multi-substrate Reactions
138
2.7
Derivation of Rate Equations of Complex Enzyme Mechanisms
138
2.7.1
King-Altmann Method
138
2.7.2
Simplified Derivations Applying Graph Theory
144
2.7.3
Combination of Equilibrium and Steady State Approach
145
2.8
Kinetic Treatment of Allosteric Enzymes
147
2.8.1
Hysteretic Enzymes
148
2.8.2
Kinetic Cooperativity, the Slow Transition Model
249
2.9 pH
and Temperature Dependence of Enzymes
151
2.9.1 pH
Optimum and Determination of pK Values
151
2.9.2 pH
Stability
153
2.9.3
Temperature Dependence
154
2.10
Isotope Exchange
158
2.10.1
Isotope Exchange Kinetics
159
2.10.2
Isotope Effects
163
2.10.2.1
Primary Kinetic Isotope Effect
163
2.10.2.2
Influence of the Kinetic Isotope Effect on V and
Кш
164
2.10.2.3
Other Isotope Effects
165
2.11
Special Enzyme Mechanisms
166
2.11.1
Ribozymes
166
2.11.2
Polymer Substrates
167
2.11.3
Kinetics of Immobilized Enzymes
168
2.11.3.1
External Diffusion Limitation
169
2.11.3.2
Internal Diffusion limitation
172
2.11.3.3
Inhibition of Immobilized Enzymes
173
2.11.3.4 pH
and Temperature Behavior of Immobilized Enzymes
174
2.11.4
Transport Processes
175
2.11.5
Enzyme Reactions at Membrane Interfaces
178
2.12
Application of Statistical Methods in Enzyme Kinetics
185
2.12.1
General Remarks
185
XIV
I Contents
2.12.2
Statistical Terms Used in Enzyme Kinetics
189
References
190
3
Methods
195
3.1
Methods for Investigation of Multiple Equilibria
195
3.1.1
Equilibrium Dialysis and General Aspects of Binding
Measurements
197
3.1.1.1
Equilibrium Dialysis
197
3.1.1.2
Control Experiments and Sources of Error
200
3.1.1.3
Continuous Equilibrium Dialysis
203
3.1.2 Ultrafiltration 206
3.1.3
Gel Filtration
207
3.1.3.1
Batch Method
208
3.1.3.2
The Method of Hummel and Dreyer
209
3.1.3.3
Other Gel Filtration Methods
210
3.1.4
Ultracentrifugation
211
3.1.4.1
Fixed Angle Ultracentrifugation Methods
212
3.1.4.2
Sucrose Gradient Centrifugation
214
3.1.5
Surface Plasmon Resonance
218
3.2
Electrochemical Methods
219
3.2.1
The Oxygen Electrode
220
3.2.2
The CO2 Electrode
222
3.2.3
Potentiometry,
Redox
Potentials
223
3.2.4
The pH-stat
223
3.2.5
Polarography
225
3.3
Calorimetry
226
3.4
Spectroscopie
Methods
228
3.4.1
Absorption Spectroscopy
230
3.4.1.1
The Lambert-Beer Law
230
3.4.1.2
Spectral Properties of Enzymes and Ligands
231
3.4.1.3
Structure of Spectrophotometers
235
3.4.1.4
Double Beam Spectrophotometer
237
3.4.1.5
Difference Spectroscopy
238
3.4.1.6
The Dual Wavelength Spectrophotometer
241
3.4.1.7
Photochemical Action Spectra
242
3.4.2
Bioluminescence
243
3.4.3
Fluorescence
243
3.4.3.1
Quantum Yield
243
3.4.3.2
Structure of Spectrofluorimeters
244
3.4.3.3
Perturbations of Fluorescence Measurements
246
3.4.3.4
Fluorescent Compounds (Fluorophores)
247
3.4.3.5
Radiationless Energy Transfer
252
3.4.3.6
Fluorescence Polarization
254
3.4.3.7
Pulse Fluorimetry
255
Contents
XV
3.4.4
Circular
Dichroism
and Optical Rotation Dispersion
257
3.4.5
Infrared and Raman Spectroscopy
262
3.4.5.1
IR
Spectroscopy
263
3.4.5.2
Raman Spectroscopy
263
3.4.5.3
Applications
264
3.4.6
Electron Paramagnetic Resonance Spectroscopy
264
3.5
Measurement of Fast Reactions
267
3.5.1
Flow Methods
268
3.5.1.1
The Continuous Flow Method
268
3.5.1.2
The Stopped-flow Method
273
3.5.1.3
Measurement of Enzyme Reactions by Flow Methods
274
3.5.1.4
Determination of the Dead Time
276
3.5.2
Relaxation Methods
277
3.5.2.1
The Temperature Jump Method
278
3.5.2.2
The Pressure Jump Method
281
3.5.2.3
The Electric Field Method
283
3.5.3
Flash Photolysis, Pico- and Femto-second Spectroscopy
283
3.5.4
Evaluation of Rapid Kinetic Reactions (Transient Kinetics)
285
References
289
Subject Index
293 |
adam_txt |
XI
Contents
Preface
to the Second English Edition
VII
Prefece
to the First English Edition IX
Symbols and Abbreviations
XVII
Introduction and Definitions
1
References
4
1
Multiple Equilibria
7
1.1
Diffusion
8
1.2
Interaction between Macromolecules and Ligands
12
1.2.1
Binding Constants
12
1.2.2
Macromolecules with One Binding Site
13
1.3
Macromolecules with Identical Independent Binding Sites
14
1.3.1
General Binding Equation
14
1.3.2
Graphic Representations of the Binding Equation
20
1.3.2.1
Direct and Linear Diagrams
20
1.3.2.2
Analysis of Binding Data from
Spectroscopie
Titrations 22
1.3.3
Binding of Different Ligands, Competition
25
1.3.4
Non-competitive Binding
27
1.4
Macromolecules with Non-identical, Independent Binding Sites
29
1.5
Macromolecules with Identical, Interacting Binding Sites,
Cooperativity
32
1.5.1
The Hill Equation
32
1.5.2
The Adair Equation
34
1.5.3
The Pauling Model
37
1.5.4
Allosteric Enzymes
38
1.5.5
The Symmetry or Concerted Model
39
1.5.6
The Sequential Model and Negative Cooperativity
44
1.5.7
Analysis of Cooperativity
48
1.5.8
Physiological Aspects of Cooperativity
50
1.5.9
Examples of Allosteric Enzymes
52
Enzyme Kinetics. Principles and Methods.
2nå
Ш.
Hans Bisswanger
Copyright
© 2008
WILEY-VCH
Verlag
GmbH
&
Co. KGaA, Weinheim
ISBN:
978-3-527-31957-2
XII Contents
1.5.9.1
Hemoglobin
52
1.5.9.2
Aspartate
Transcarbamoylase
53
1.5.9.3 Aspartokinase 54
1.5.9.4 Phosphofractokinase 55
1.5.9.5 Allosteric Regulation
of the
Glycogen
Metabolism
55
1.5.9.6 Membrane
Bound Enzymes and Receptors
55
1.6
Non-identical, Interacting Binding Sites
56
References
57
2
Enzyme Kinetics
59
2.1
Reaction Order
59
2.1.1
First Order Reactions
60
2.1.2
Second Order Reactions
61
2.1.3
Zero Order Reactions
62
2.2
Steady-State Kinetics and the Michaelis-Menten Equation
63
2.2.1
Derivation of the Michaelis-Menten Equation
63
2.3
Analysis of Enzyme Kinetic Data
66
2.3.1
Graphical Representations of the Michaelis-Menten Equation
66
2.3.1.1
Direct and Semi-logarithmic Representations
66
2.3.1.2
Direct Linear Plots
73
2.3.1.3
Linearization Methods
75
2.3.2
Analysis of Progress Curves
77
2.3.2.1
Integrated Michaelis-Menten Equation
78
2.3.2.2
Determination of Reaction Rates
80
2.3.2.3
Graphic Methods for Rate Determination
82
2.3.2.4
Graphic Determination of True Initial Rates
84
2.4
Reversible Enzyme Reactions
85
2.4.1
Rate Equation for Reversible Enzyme Reactions
85
2.4.2
The Haldane Relationship
87
2.4.3
Product Inhibition
88
2.5
Enzyme Inhibition
91
2.5.1
Unspecific Enzyme Inhibition
91
2.5.2
Irreversible Enzyme Inhibition
92
2.5.2.1
General Features of Irreversible Enzyme Inhibition
92
2.5.2.2
Suicide Substrates
93
2.5.2.3
Transition State Analogs
95
2.5.2.4
Analysis of Irreversible Inhibitions
96
2.5.3
Reversible Enzyme Inhibition
98
2.5.3.1
General Rate Equation
98
2.5.3.2
Non-Competitive Inhibition and Graphic Representation
of Inhibition Data
101
2.5.3.3
Competitive Inhibition
107
2.5.3.4
Uncompetitive Inhibition 111
2.5.3.5
Partially Non-competitive Inhibition
113
Contents XIII
2.5.3.6
Partially Uncompetitive Inhibition
115
2.5.3.7
Partially Competitive Inhibition
117
2.5.3.8
Noncompetitive
and Uncompetitive Product Inhibition
119
2.5.3.9
Substrate Inhibition
120
2.5.4
Enzyme Reactions with Two Competing Substrates
121
2.5.5
Different Enzymes Catalyzing the Same Reaction
123
2.6
Multi-substrate Reactions
124
2.6.1
Nomenclature
124
2.
ii.
2
Random Mechanism
126
2.6.3
Ordered Mechanism
131
2.6.4
Ping-pong Mechanism
132
2.6.5
Product Inhibition in Multi-substrate Reactions
135
2.6.6
Haldane Relationships in Multi-substrate Reactions
135
2.6.7
Mechanisms with more than Two Substrates
136
2.6.8
Other Nomenclatures for Multi-substrate Reactions
138
2.7
Derivation of Rate Equations of Complex Enzyme Mechanisms
138
2.7.1
King-Altmann Method
138
2.7.2
Simplified Derivations Applying Graph Theory
144
2.7.3
Combination of Equilibrium and Steady State Approach
145
2.8
Kinetic Treatment of Allosteric Enzymes
147
2.8.1
Hysteretic Enzymes
148
2.8.2
Kinetic Cooperativity, the Slow Transition Model
249
2.9 pH
and Temperature Dependence of Enzymes
151
2.9.1 pH
Optimum and Determination of pK Values
151
2.9.2 pH
Stability
153
2.9.3
Temperature Dependence
154
2.10
Isotope Exchange
158
2.10.1
Isotope Exchange Kinetics
159
2.10.2
Isotope Effects
163
2.10.2.1
Primary Kinetic Isotope Effect
163
2.10.2.2
Influence of the Kinetic Isotope Effect on V and
Кш
164
2.10.2.3
Other Isotope Effects
165
2.11
Special Enzyme Mechanisms
166
2.11.1
Ribozymes
166
2.11.2
Polymer Substrates
167
2.11.3
Kinetics of Immobilized Enzymes
168
2.11.3.1
External Diffusion Limitation
169
2.11.3.2
Internal Diffusion limitation
172
2.11.3.3
Inhibition of Immobilized Enzymes
173
2.11.3.4 pH
and Temperature Behavior of Immobilized Enzymes
174
2.11.4
Transport Processes
175
2.11.5
Enzyme Reactions at Membrane Interfaces
178
2.12
Application of Statistical Methods in Enzyme Kinetics
185
2.12.1
General Remarks
185
XIV
I Contents
2.12.2
Statistical Terms Used in Enzyme Kinetics
189
References
190
3
Methods
195
3.1
Methods for Investigation of Multiple Equilibria
195
3.1.1
Equilibrium Dialysis and General Aspects of Binding
Measurements
197
3.1.1.1
Equilibrium Dialysis
197
3.1.1.2
Control Experiments and Sources of Error
200
3.1.1.3
Continuous Equilibrium Dialysis
203
3.1.2 Ultrafiltration 206
3.1.3
Gel Filtration
207
3.1.3.1
Batch Method
208
3.1.3.2
The Method of Hummel and Dreyer
209
3.1.3.3
Other Gel Filtration Methods
210
3.1.4
Ultracentrifugation
211
3.1.4.1
Fixed Angle Ultracentrifugation Methods
212
3.1.4.2
Sucrose Gradient Centrifugation
214
3.1.5
Surface Plasmon Resonance
218
3.2
Electrochemical Methods
219
3.2.1
The Oxygen Electrode
220
3.2.2
The CO2 Electrode
222
3.2.3
Potentiometry,
Redox
Potentials
223
3.2.4
The pH-stat
223
3.2.5
Polarography
225
3.3
Calorimetry
226
3.4
Spectroscopie
Methods
228
3.4.1
Absorption Spectroscopy
230
3.4.1.1
The Lambert-Beer Law
230
3.4.1.2
Spectral Properties of Enzymes and Ligands
231
3.4.1.3
Structure of Spectrophotometers
235
3.4.1.4
Double Beam Spectrophotometer
237
3.4.1.5
Difference Spectroscopy
238
3.4.1.6
The Dual Wavelength Spectrophotometer
241
3.4.1.7
Photochemical Action Spectra
242
3.4.2
Bioluminescence
243
3.4.3
Fluorescence
243
3.4.3.1
Quantum Yield
243
3.4.3.2
Structure of Spectrofluorimeters
244
3.4.3.3
Perturbations of Fluorescence Measurements
246
3.4.3.4
Fluorescent Compounds (Fluorophores)
247
3.4.3.5
Radiationless Energy Transfer
252
3.4.3.6
Fluorescence Polarization
254
3.4.3.7
Pulse Fluorimetry
255
Contents
XV
3.4.4
Circular
Dichroism
and Optical Rotation Dispersion
257
3.4.5
Infrared and Raman Spectroscopy
262
3.4.5.1
IR
Spectroscopy
263
3.4.5.2
Raman Spectroscopy
263
3.4.5.3
Applications
264
3.4.6
Electron Paramagnetic Resonance Spectroscopy
264
3.5
Measurement of Fast Reactions
267
3.5.1
Flow Methods
268
3.5.1.1
The Continuous Flow Method
268
3.5.1.2
The Stopped-flow Method
273
3.5.1.3
Measurement of Enzyme Reactions by Flow Methods
274
3.5.1.4
Determination of the Dead Time
276
3.5.2
Relaxation Methods
277
3.5.2.1
The Temperature Jump Method
278
3.5.2.2
The Pressure Jump Method
281
3.5.2.3
The Electric Field Method
283
3.5.3
Flash Photolysis, Pico- and Femto-second Spectroscopy
283
3.5.4
Evaluation of Rapid Kinetic Reactions (Transient Kinetics)
285
References
289
Subject Index
293 |
any_adam_object | 1 |
any_adam_object_boolean | 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 | BV023128164 |
callnumber-first | Q - Science |
callnumber-label | QP601 |
callnumber-raw | QP601.3 |
callnumber-search | QP601.3 |
callnumber-sort | QP 3601.3 |
callnumber-subject | QP - Physiology |
classification_rvk | WC 4350 WD 5050 |
classification_tum | CHE 827f |
ctrlnum | (OCoLC)225406378 (DE-599)DNB986185752 |
dewey-full | 572/.744 |
dewey-hundreds | 500 - Natural sciences and mathematics |
dewey-ones | 572 - Biochemistry |
dewey-raw | 572/.744 |
dewey-search | 572/.744 |
dewey-sort | 3572 3744 |
dewey-tens | 570 - Biology |
discipline | Biologie Chemie |
discipline_str_mv | Biologie Chemie |
edition | 2., rev. and updated ed. |
format | Book |
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id | DE-604.BV023128164 |
illustrated | Illustrated |
index_date | 2024-07-02T19:54:14Z |
indexdate | 2024-07-20T09:32:37Z |
institution | BVB |
isbn | 9783527319572 3527319573 |
language | English German |
oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-016330545 |
oclc_num | 225406378 |
open_access_boolean | |
owner | DE-91G DE-BY-TUM DE-20 DE-355 DE-BY-UBR DE-703 DE-634 DE-83 DE-91S DE-BY-TUM DE-11 DE-M49 DE-BY-TUM |
owner_facet | DE-91G DE-BY-TUM DE-20 DE-355 DE-BY-UBR DE-703 DE-634 DE-83 DE-91S DE-BY-TUM DE-11 DE-M49 DE-BY-TUM |
physical | XVIII, 301 S. graph. Darst. 240 mm x 170 mm |
publishDate | 2008 |
publishDateSearch | 2008 |
publishDateSort | 2008 |
publisher | WILEY-VCH |
record_format | marc |
spelling | Bisswanger, Hans 1943- Verfasser (DE-588)129060461 aut Enzyme kinetics principles and methods Hans Bisswanger 2., rev. and updated ed. Weinheim WILEY-VCH 2008 XVIII, 301 S. graph. Darst. 240 mm x 170 mm txt rdacontent n rdamedia nc rdacarrier Früher mit der Nummer 9783527303434 Cinétique enzymatique Cinétique enzymatique - Méthodologie Enzyme kinetics Enzymes metabolism Kinetics Methode (DE-588)4038971-6 gnd rswk-swf Enzymkinetik (DE-588)4133166-7 gnd rswk-swf Enzymkinetik (DE-588)4133166-7 s Methode (DE-588)4038971-6 s 1\p DE-604 http://d-nb.info/986185752/04 Inhaltsverzeichnis text/html http://deposit.dnb.de/cgi-bin/dokserv?id=3018887&prov=M&dok_var=1&dok_ext=htm Inhaltstext Digitalisierung UB Regensburg application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=016330545&sequence=000002&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- Enzyme kinetics principles and methods Cinétique enzymatique Cinétique enzymatique - Méthodologie Enzyme kinetics Enzymes metabolism Kinetics Methode (DE-588)4038971-6 gnd Enzymkinetik (DE-588)4133166-7 gnd |
subject_GND | (DE-588)4038971-6 (DE-588)4133166-7 |
title | Enzyme kinetics principles and methods |
title_auth | Enzyme kinetics principles and methods |
title_exact_search | Enzyme kinetics principles and methods |
title_exact_search_txtP | Enzyme kinetics principles and methods |
title_full | Enzyme kinetics principles and methods Hans Bisswanger |
title_fullStr | Enzyme kinetics principles and methods Hans Bisswanger |
title_full_unstemmed | Enzyme kinetics principles and methods Hans Bisswanger |
title_short | Enzyme kinetics |
title_sort | enzyme kinetics principles and methods |
title_sub | principles and methods |
topic | Cinétique enzymatique Cinétique enzymatique - Méthodologie Enzyme kinetics Enzymes metabolism Kinetics Methode (DE-588)4038971-6 gnd Enzymkinetik (DE-588)4133166-7 gnd |
topic_facet | Cinétique enzymatique Cinétique enzymatique - Méthodologie Enzyme kinetics Enzymes metabolism Kinetics Methode Enzymkinetik |
url | http://d-nb.info/986185752/04 http://deposit.dnb.de/cgi-bin/dokserv?id=3018887&prov=M&dok_var=1&dok_ext=htm http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=016330545&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
work_keys_str_mv | AT bisswangerhans enzymekineticsprinciplesandmethods |
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