Practical enzymology:
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| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Weinheim
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[2019]
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| Ausgabe: | Third edition |
| Schlagworte: | |
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| Beschreibung: | xviii, 393 Seiten Illustrationen, Diagramme |
| ISBN: | 9783527346042 |
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| 084 | |a CHE 828f |2 stub | ||
| 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 Third edition | ||
| 264 | 1 | |a Weinheim |b Wiley-VCH |c [2019] | |
| 264 | 4 | |c © 2019 | |
| 300 | |a xviii, 393 Seiten |b Illustrationen, Diagramme | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 650 | 0 | 7 | |a Enzymkinetik |0 (DE-588)4133166-7 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Enzym |0 (DE-588)4014988-2 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Enzymtechnologie |0 (DE-588)4135962-8 |2 gnd |9 rswk-swf |
| 653 | |a Biochemie | ||
| 653 | |a Biochemie u. Chemische Biologie | ||
| 653 | |a Biochemistry | ||
| 653 | |a Biowissenschaften | ||
| 653 | |a Cellular & Molecular Medicine | ||
| 653 | |a Chemie | ||
| 653 | |a Chemistry | ||
| 653 | |a Life Sciences | ||
| 653 | |a Medical Science | ||
| 653 | |a Medizin | ||
| 653 | |a Zell- u. Molekularmedizin | ||
| 655 | 7 | |0 (DE-588)4127380-1 |a Praktikum |2 gnd-content | |
| 689 | 0 | 0 | |a Enzymtechnologie |0 (DE-588)4135962-8 |D s |
| 689 | 0 | 1 | |a Enzymkinetik |0 (DE-588)4133166-7 |D s |
| 689 | 0 | |5 DE-604 | |
| 689 | 1 | 0 | |a Enzym |0 (DE-588)4014988-2 |D s |
| 689 | 1 | |8 1\p |5 DE-604 | |
| 776 | 0 | 8 | |i Erscheint auch als |n Online-Ausgabe, PDF |z 978-3-527-82081-8 |
| 776 | 0 | 8 | |i Erscheint auch als |n Online-Ausgabe, EPUB |z 978-3-527-82080-1 |
| 776 | 0 | 8 | |i Erscheint auch als |n Online-Ausgabe |z 978-3-527-82078-8 |
| 856 | 4 | 2 | |m DNB Datenaustausch |q application/pdf |u http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031325876&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
| 999 | |a oai:aleph.bib-bvb.de:BVB01-031325876 | ||
| 883 | 1 | |8 1\p |a cgwrk |d 20201028 |q DE-101 |u https://d-nb.info/provenance/plan#cgwrk | |
Datensatz im Suchindex
| _version_ | 1804180146516656128 |
|---|---|
| adam_text | V
CONTENTS
PREFACE
TO
THE
THIRD
EDITION
XV
LIST
OF
ABBREVIATIONS
AND
SYMBOLS
XVII
1
GENERAL
ASPECTS
OF
ENZYME
ANALYSIS
1
1.1
INTRODUCTION
AND
ESSENTIALS
FOR
ENZYME
ASSAYS
1
STANDARD
BOOKS,
SERIES
4
DATABASES
4
1.2
THEORETICAL
BASIS
OF
ENZYME
ASSAYS
4
1.2.1
ORDER
OF
ENZYME
REACTIONS
4
1.2.2
IMPORTANCE
OF
THE
REACTION
ORDER
FOR
ENZYME
REACTIONS
6
1.2.3
THE
REACTION
VELOCITY,
SIGNIFICANCE,
AND
PRACTICAL
ASPECTS
10
1.2.3.1
DETERMINATION
OF
THE
REACTION
VELOCITY,
THE
PROGRESS
CURVE
10
1.2.3.2
ENZYME
UNITS
15
1.2.3.3
A
SHORT
DISCUSSION
ABOUT
ERRORS
IN
ENZYME
ASSAYS
17
1.2.3.4
PRACTICAL
RULES
FOR
THE
PREPARATION
OF
DILUTION
SERIES
21
1.2.3.5
STATISTICAL
TREATMENT
OF
ENZYME
REACTIONS
23
1.2.4
TREATMENT
OF
THE
MICHAELIS-MENTEN
EQUATION
24
1.2.4.1
GENERAL
CONSIDERATIONS
24
1.2.4.2
LINEAR
REPRESENTATIONS
OF
THE
MICHAELIS-MENTEN
EQUATION
26
1.2.5
ENZYME
INHIBITION
28
1.2.6
MULTISUBSTRATE
REACTIONS
33
1.3
ESSENTIAL
CONDITIONS
FOR
ENZYME
ASSAYS
35
1.3.1
DEPENDENCE
ON
SOLVENTS
AND
IONIC
STRENGTH
35
1.3.2
PH
DEPENDENCY
36
1.3.2.1
ISOELECTRIC
POINT
38
1.3.2.2
BUFFERS:
WHAT
MUST
BE
REGARDED?
38
1.3.2.3
HOW
TO
PREPARE
BUFFERS?
41
1.3.3
TEMPERATURE
DEPENDENCY
42
1.3.4
STABILITY
OF
ENZYMES
47
1.3.4.1
WHY
ARE
ENZYMES
UNSTABLE?
47
1.3.4.2
HOW
CAN
ENZYMES
BE
STABILIZED?
48
1.3.4.3
HOW
TO
STORE
ENZYMES?
48
1.4
THEORY
OF
COUPLED
ENZYME
REACTIONS
51
1.4.1
TWO
COUPLED
REACTIONS
51
1.4.2
THREE
COUPLED
REACTIONS
54
1.5
SUBSTRATE
DETERMINATION
54
VI
CONTENTS
1.5.1
1.5.2
1.5.3
1.5.4
END
POINT
METHOD
55
SUBSTRATE
DETERMINATION
BY
COUPLED
ENZYME
REACTIONS
56
KINETIC
METHOD
FOR
SUBSTRATE
DETERMINATION
57
ENZYMATIC
CYCLING
57
2
2.1
2.1.1
2.1.2
2.1.2.1
2.1.2.2
2.1.2.3
2.1.3
2.1.4
2.1.5
2.1.6
2.2
2.2.1
2.2.2
2.2.3
2.2.4
2.3
2.4
INSTRUMENTAL
ASPECTS
61
SPECTROSCOPIC
METHODS
61
ABSORPTION
(UV/VIS)
PHOTOMETRY
61
CUVETTES
72
SHAPE
72
MATERIAL
73
CLEANING
73
TURBIDITY
MEASUREMENT
74
FLUORESCENCE
PHOTOMETRY
75
LUMINOMETRY
79
POLARIMETRY
80
ELECTROCHEMICAL
METHODS
81
PH
METER
AND
GLASS
ELECTRODES
81
PH
STAT
82
POTENTIOMETRY
83
OXYGEN
AND
CARBON
DIOXIDE
ELECTRODES
83
RADIOACTIVE
LABELING
84
DIVERSE
METHODS
84
3
3.1
3.2
ENZYME
ASSAYS
87
ENZYME
NOMENCLATURE
88
PRACTICAL
CONSIDERATIONS
FOR
ENZYME
ASSAYS
90
4
4.1
4.1.1
4.1.2
4.2
4.2.1
4.2.2
4.3
4.4
4.5
4.6
4.6.1
4.6.2
4.6.3
4.7
4.8
OXIDOREDUCTASES,
EC
1
95
GENERAL
ASSAY
PROCEDURES
95
OPTICAL
ASSAY
95
FLUORIMETRIC
ASSAY
96
ALCOHOL
DEHYDROGENASE
(ADH),
EC
1.1.1.1
96
REDUCTION
ASSAY
96
OXIDATION
ASSAY
97
ALCOHOL
DEHYDROGENASE
(NADP
+
),
EC
1.1.1.2
98
HOMOSERINE
DEHYDROGENASE,
EC
1.1.1.3
99
SHIKIMATE
DEHYDROGENASE,
EC
1.1.1.25
100
L-LACTATE
DEHYDROGENASE
(LDH),
EC
1.1.1.27
101
PHOTOMETRIC
REDUCTION
ASSAY
101
FLUORIMETRIC
REDUCTION
ASSAY
102
OXIDATION
ASSAY
103
MALATE
DEHYDROGENASE
(MDH),
EC
1.1.1.37
104
MALATE
DEHYDROGENASE
(OXALOACETATE-DECARBOXYLATING)
(NAD
+
),
EC
1.1.1.38,
AND
MALATE
DEHYDROGENASE
(DECARBOXYLATING),
EC
1.1.1.39
105
CONTENTS
VII
4.9
MALATE
DEHYDROGENASE
(OXALOACETATE-DECARBOXYLATING)
(NADP
+
),
EC
1.1.1.40
106
4.10
ISOCITRATE
DEHYDROGENASE
(NAD
+
)
(ICDH),
EC
1.1.1.41
107
4.11
ISOCITRATE
DEHYDROGENASE
(NADP
+
)
(ICDH),
EC
1.1.1.42
108
4.12
GLUCOSE-6-PHOSPHATE
DEHYDROGENASE
(NADP
+
),
EC
1.1.1.49
(G6PDH)
109
4.13
GLUCOSE
OXIDASE
(GOD),
EC
1.1.3.4
110
4.14
FORMATE
DEHYDROGENASE
(FDH),
EC
1.2.1.2
111
4.15
GLYCERALDEHYDE-3-PHOSPHATE
DEHYDROGENASE
(GAPDH),
EC
1.2.1.12
112
4.15.1
OXIDATION
ASSAY
112
4.15.2
REDUCTION
ASSAY
COUPLED WITH
3-PHOSPHOGLYCERATE
KINASE
(PGK)
113
4.16
LONG-CHAIN-ALDEHYDE
DEHYDROGENASE,
EC
1.2.1.48
114
4.17
PYRUVATE
DEHYDROGENASE
(ACETYL-TRANSFERRING)
(PDH),
EC
1.2.4.1
116
4.17.1
FERRICYANIDE
AS
ELECTRON ACCEPTOR
116
4.17.2
DICHLOROPHENOLINDOPHENOL
AS
ELECTRON
ACCEPTOR
117
4.18
ALDEHYDE
OXIDASE,
EC
1.2.3.1
118
4.19
OXOGLUTARATE
DEHYDROGENASE
(SUCCINYL-TRANSFERRING)
(OGDH),
EC
1.2.4.2
119
4.20
PYRUVATE
FERREDOXIN
OXIDOREDUCTASE,
EC
1.2.7.1
120
4.20.1
ASSAY
WITH
CYTOCHROME
C
(CYT
C)
AS
ELECTRON ACCEPTOR
121
4.21
ALANINE
DEHYDROGENASE,
EC
1.4.1.1
121
4.21.1
OXIDATION
OF
ALANINE
122
4.21.2
REDUCTION
OF
PYRUVATE
122
4.22
GLUTAMATE
DEHYDROGENASE,
EC
1.4.1.3
123
4.23
LEUCINE
DEHYDROGENASE,
EC
1.4.1.9
124
4.24
L
-
AMINO-ACID
OXIDASE,
EC
1.4.3.2
125
4.25
D-AMINO-ACID
OXIDASE,
EC
1.4.3.3
126
4.26
MONOAMINE
OXIDASE,
EC
1.4.3.4
126
4.27
PRIMARY
AMINE
OXIDASE,
EC
1.4.3.21
127
4.27.1
SPECTROPHOTOMETRIC
ASSAY
128
4.27.2
POLAROGRAPHIC
ASSAY
OF
O
2
UPTAKE
WITH
O
2
ELECTRODE
128
4.27.3
ASSAYS
FOR
BENZYLAMINE
OXIDASE
ACTIVITY
129
4.28
DIAMINE
OXIDASE,
EC
1.4.3.22
129
4.29
NADH:UBIQUINONE
REDUCTASE
(H
+
-TRANSLOCATING)
EC
1.6.5.3
130
4.29.1
SPECTROPHOTOMETRIC
ASSAY
131
4.30
NADH
DEHYDROGENASE,
EC
1.6.99.3
131
4.31
FACTOR-INDEPENDENT
URATE
HYDROXYLASE,
EC
1.7.3.3
132
4.32
DIHYDROLIPOYL
DEHYDROGENASE,
EC
1.8.1.4
133
4.32.1
OXIDATION
OF
DIHYDROLIPOAMIDE
134
4.32.2
REDUCTION
OF
LIPOAMIDE
134
4.33
GLUTATHIONE
DISULFIDE
REDUCTASE,
EC
1.8.1.7
135
4.34
CYTOCHROME-C
OXIDASE
(COX),
EC
1.9.3.1
137
4.34.1
SPECTROPHOTOMETRIC
ASSAY
137
4.34.2
ASSAY
WITH
OXYGEN
ELECTRODE
137
4.35
CATALASE,
EC
1.11.1.6
138
VIII
CONTENTS
4.36
PEROXIDASE
(POD)
EC
1.11.1.7
139
4.36.1
ASSAY
WITH
2,2 -AZINO-BIS-3-ETHYLBENZOTHIAZOLINE-6-SULFONIC
ACID
(ABTS)
140
4.36.2
ASSAY
WITH
GUAIACOL
140
4.36.3
ASSAY
WITH
DIANISIDINE
141
4.37
GLUTATHIONE
PEROXIDASE,
EC
1.11.1.9
142
4.37.1
COUPLED
ASSAY
WITH
GLUTATHIONE
REDUCTASE
142
4.38
PHOTINUS
LUCIFERIN
4-MONOOXIGENASE
(ATP-HYDROLYZING),
EC
1.13.12.7
143
4.39
ALKYLGLYCEROL
MONOOXYGENASE,
EC
1.14.16.5
145
4.39.1
SPECTROSCOPIC
ASSAY
145
4.39.2
COUPLED
ASSAY
WITH
HPLC
DETECTION
145
4.40
DOPAMINE
R-MONOOXYGENASE,
EC
1.14.17.1
147
4.41
TYROSINASE,
EC
1.14.18.1
148
4.41.1
DOPA
OXIDASE
ASSAY
148
4.41.2
DOPACHROME
ASSAY
149
4.42
SUPEROXIDE
DISMUTASE
(SOD),
EC
1.15.1.1
149
4.42.1
ASSAY
WITH
PYROGALLOL
150
4.42.2
ASSAY
WITH
FERRICYTOCHROME
C
AND
XANTHINE
OXIDASE
150
4.43
XANTHINE
OXIDASE
(XOD),
EC
1.17.3.2
151
5
TRANSFERASES,
EC
2
153
5.1
ORNITHINE
CARBAMOYLTRANSFERASE
(OTC),
EC
2.1.3.3
153
5.1.1
METHOD
1
FOR
COLOR
DEVELOPMENT
154
5.1.2
METHOD
2
FOR
COLOR
DEVELOPMENT
154
5.2
CHOLINE
O-ACETYLTRANSFERASE,
EC
2.3.1.6
155
5.3
CARNITINE
O-ACETYLTRANSFERASE,
EC
2.3.1.7
156
5.3.1
DIRECT
SPECTROSCOPIC
ASSAY
156
5.3.2
ASSAY
WITH
DTNB
157
5.4
DIHYDROLIPOAMIDE
ACETYLTRANSFERASE,
EC
2.3.1.12
157
5.4.1
SPECTROPHOTOMETRIC
ASSAY
158
5.4.2
STOPPED
ASSAY
159
5.5
FATTY
ACID
SYNTHASE,
EC
2.3.1.85
160
5.6
Y
-GLUTAMYLTRANSFERASE,
EC
2.3.2.2
161
5.7
CITRATE
SYNTHASES,
EC
2.3.3.1,
EC
2.3.3.3,
AND
EC
2.3.3.16
162
5.8
ATP
CITRATE
LYASE,
EC
2.3.3.S
164
5.9
GLYCOGEN
PHOSPHORYLASE,
EC
2.4.1.1
165
5.10
PURINE-NUCLEOSIDE
PHOSPHORYLASE
(PNP),
EC
2.4.2.1
166
5.11
GLUTATHIONE
TRANSFERASE,
EC
2.5.1.18
167
5.11.1
SPECTROPHOTOMETRIC
ASSAY
168
5.11.2
TITRIMETRIC
ASSAY
168
5.12
ASPARTATE
TRANSAMINASE
(AAT),
EC
2.6.1.1
169
5.13
ALANINE
TRANSAMINASE,
EC
2.6.1.2
170
5.14
TYROSINE
TRANSAMINASE
(TAT),
EC
2.6.1.5;
TRYPTOPHAN
TRANSAMINASE
(TAM
1),
EC
2.6.1.27;
PHENYLALANINE
(HISTIDINE)
TRANSAMINASE,
EC
2.6.1.58
171
5.14.1
TYROSINE
TRANSAMINASE
171
CONTENTS
IX
5.14.2
5.14.3
5.15
5.16
5.17
5.18
5.19
5.20
5.20.1
5.20.2
TRYPTOPHAN
TRANSAMINASE
171
PHENYLALANINE
(HISTIDINE)
TRANSAMINASE:
171
HEXOKINASE
(HK),
EC
2.7.1.1,
GLUCOKINASE
(GK),
EC
2.7.1.2
173
PYRUVATE
KINASE
(PK),
EC
2.7.1.40
174
ACETATE
KINASE,
EC
2.7.2.1
176
PHOSPHOGLYCERATE
KINASE
(PGK),
EC
2.7.2.3
177
ASPARTATE
KINASE
(AK),
EC
2J7.2.4
178
CREATINE
KINASE
(CK),
EC
2.7.3.2
180
COUPLED
ASSAY
180
PH-COLORIMETRIC
ASSAY
181
6
6.1
6.1.1
6.1.2
6.2
6.3
6.4
6.4.1
6.4.2
6.5
6.5.1
6.5.2
6.6
6.7
6.7.1
6.7.2
6.8
6.9
6.9.1
6.9.2
6.10
6.11
6.12
6.13
6.14
6.15
6.15.1
6.15.2
6.15.3
6.16
6.16.1
6.16.2
6.16.3
6.16.4
6.17
6.18
HYDROLASES,
EC
3
183
TRIACYLGLYCEROL
LIPASE,
EC
3.1.1.3
183
ASSAY
WITH
PH
STAT
(AUTO-TITRATOR)
183
FLUORIMETRIC
ASSAY
184
PHOSPHOLIPASE
A
2
,
EC
3.1.1.4
185
ACETYLCHOLINESTERASE
(ACHE),
EC
3.1.1.7
186
CHOLINESTERASE
(BUTCHE),
EC
3.1.1.8
187
PH
STAT
ASSAY
187
COLORIMETRIC
ASSAY
188
HYDROXYACYLGLUTATHIONE
HYDROLASE,
EC
3.1.2.6
189
DIRECT
ASSAY
189
ASSAY
WITH
DTNB
189
S-FORMYLGLUTATHIONE
HYDROLASE,
EC
3.1.2.12
190
ALKALINE
PHOSPHATASE,
EC
3.1.3.1
191
MAMMALIAN
ALKALINE
PHOSPHATASE
191
BACTERIAL
ALKALINE
PHOSPHATASE
192
ACID
PHOSPHATASE,
EC
3.1.3.2
192
5
-NUCLEOTIDASE,
EC
3.1.3.5
193
ASSAY
BY
DETERMINATION
OF
PJ
194
ASSAY
BY
CONVERTING
ADENOSINE
INTO
INOSINE
194
GLUCOSE-6-PHOSPHATASE,
EC
3.1.3.9
195
3 ,5 -CYCLIC-NUCLEOTIDE
PHOSPHODIESTERASE,
EC
3.1.4.17
196
STERYL-SULFATASE,
EC
3.1.6.2
198
PANCREATIC
RIBONUCLEASE,
EC
3.1.27.5
198
A-AMYLASE,
EC
3.2.1.1
199
GLUCAN
1,4-A-GLUCOSIDASE
(AMG),
EC
3.2.1.3
201
COUPLED
ASSAY
WITH
HK
AND
G6PDH
201
PHOTOMETRIC
ASSAY
WITH
4-NITROPHENYL-D-GLUCOSE
202
FLUORIMETRIC
ASSAY
WITH
4-METHYLUMBELLIFERYL-A-D-GLUCOSIDE
202
CELLULASES
203
0-1,4-GLUCANASE,
EC
3.2.1.4
203
P-GLUCOSIDASE,
EC
3.2.1.21
203
ORCINOL
ASSAY
204
ACTIVITY
STAINING
204
LYSOZYM,
EC
3.2.1.17
206
SIALIDASE,
EC
3.2.1.18
207
X
CONTENTS
6.18.1
FLUORIMETRIC
ASSAY
207
6.18.2
ACTIVITY
STAINING
208
6.19
A-GLUCOSIDASE,
EC
3.2.1.20
208
6.19.1
COUPLED
ASSAY
208
6.19.1.1
A-GLUCOSIDASE
REACTION
209
6.19.1.2
GLUCOSE
DETERMINATION
209
6.19.2
ASSAY
WITH
4-NITROPHENYLGLUCOPYRANOSIDE
210
6.20
P-GALACTOSIDASE,
EC
3.2.1.23
211
6.21
OC-MANNOSIDASE,
EC
3.2.1.24
212
6.21.1
PHOTOMETRIC
MICROASSAY
212
6.21.2
FLUORIMETRIC
ASSAY
213
6.22
P-FRUCTOFURANOSIDASE,
EC
3.2.1.26
213
6.23
P-GLUCURONIDASE,
EC
3.2.1.31
214
6.23.1
FLUORIMETRIC
ASSAY
215
6.24
PJV-ACETYLHEXOSAMINIDASE,
EC
3.2.1.52
215
6.25
PROTEASES,
EC
3.4,
GENERAL
ASSAYS
216
6.25.1
ANSON
ASSAY
216
6.25.2
CASEIN
ASSAY
218
6.25.3
AZOCASEIN
ASSAY
219
6.25.4
NINHYDRIN
ASSAY
220
6.26
LEUCYL
AMINOPEPTIDASE
(LAP),
EC
3.4.11.1,
BACTERIAL
LEUCYL
AMINOPEPTIDASE,
EC
3.4.11.10
221
6.26.1
ASSAY
WITH
LEUCINEAMIDE
222
6.26.2
ASSAY
WITH
LEUCINE-/2-NITROANILIDE
222
6.27
PEPTIDYL-DIPEPTIDASE
A,
EC
3.4.15.1
223
6.28
A-CHYMOTRYPSIN,
EC
3.4.21.1
224
6.28.1
ASSAY
WITH
SUPHEPA
224
6.28.2
ASSAY
WITH
GLUPHEPA
225
6.29
TRYPSIN,
EC
3.4.21.4
226
6.30
PANCREATIC
ELASTASE,
EC
3.4.21.35
227
6.30.1
ASSAY
WITH
SUCCINYL-ALA-ALA-ALA-/2-NITROANILIDE
227
6.30.2
ESTERASE
ACTIVITY
OF
ELASTASE
227
6.31
CATHEPSIN
B,
EC
3.4.22.1
228
6.32
PEPSIN
A,
EC
3.4.23.1
229
6.33
ASPARAGINASE,
EC
3.5.1.1
230
6.34
GLUTAMINASE,
EC
3.5.1.2
232
6.34.1
DETERMINATION
OF
AMMONIA
WITH
NESSLERS
REAGENT
232
6.34.2
PH
STAT
ASSAY
233
6.35
UREASE,
EC
3.5.1.5
233
6.35.1
PH
STAT
ASSAY
234
6.35.2
PHOTOMETRIC
ASSAY
234
6.36
GUANINE
DEAMINASE,
EC
3.5.4.3
235
6.36.1
DETERMINATION
OF
AMMONIA
236
6.37
ADENOSINETRIPHOSPHATASE,
EC
3.6.1.3
237
6.38
MG
2+
IMPORTING
ATPASE,
EC
3.6.3.2,
NA
+
/K
+
-EXCHANGING
ATPASE,
EC
3.6.3.9
238
6.38.1
ASSAY
OF
TOTAL
ATPASE
ACTIVITY
238
CONTENTS
XI
6.38.2
ASSAY
OF
MG
2+
-ATPASE
ACTIVITY
239
7
LYASES,
EC
4
241
7.1
PYRUVATE
DECARBOXYLASE
(PDC),
EC
4.1.1.1
241
7.2
GLUTAMATE
DECARBOXYLASE
(GAD),
EC
4.1.1.15
242
7.3
FRUCTOSE-BISPHOSPHATE
ALDOLASE,
EC
4.1.2.13
244
7.4
ANTHRANILATE
SYNTHASE,
EC
4.1.3.27
245
7.5
CARBONIC
ANHYDRASE
(CA),
EC
4.2.1.1
246
7.5.1
PH
STAT
ASSAY
246
7.5.2
ESTERASE
ASSAY
WITH
4-NITROPHENYLACETATE
247
7.6
FUMARATE
HYDRATASE,
EC
4.2.1.2
248
7.7
LACTOYLGLUTATHIONE
LYASE,
EC
4.4.1.5
249
7.8
ADENYLATE
CYCLASE
(AC),
EC
4.6.1.1
250
8
ISOMERASES,
EC
5
253
8.1
XYLOSE
ISOMERASE,
EC
5.3.1.5
253
8.1.1
D-XYLOSE
ISOMERASE
ASSAY
253
8.1.2
D-XYLOSE
ISOMERASE
MICROPLATE
ASSAY
254
8.1.3
D-GLUCOSE
ISOMERASE
ASSAY
255
8.1.4
D-GLUCOSE
ISOMERASE
MICROPLATE
ASSAY
256
8.2
GLUCOSE-6-PHOSPHATE
ISOMERASE
(G6PI),
EC
5.3.1.9
256
8.3
PHOSPHOGLUCOMUTASE
(PGM),
EC
5.4.2.2
257
9
LIGASES
(SYNTHETASES),
EC
6
261
9.1
TYROSINE-TRNA
LIGASE,
EC
6.1.1.1
261
9.1.1
FLUORIMETRIC
ASSAY
261
9.1.2
ATP-
32
PP
EXCHANGE
262
9.2
ACETATE-COA
LIGASE
(ACL),
EC
6.2.1.1
263
9.2.1
DIRECT
RADIOACTIVE
ASSAY
264
9.2.2
COUPLED
SPECTROSCOPIC
ASSAY
264
9.3
GLUTAMINE
SYNTHETASE,
EC
6.3.1.2
266
10
ASSAYS
FOR
MULTI-ENZYME
COMPLEXES
269
10.1
PYRUVATE
DEHYDROGENASE
COMPLEX
(PDHC)
269
10.1.1
OVERALL
ACTIVITY
OF
PDHC
BY
NAD
+
REDUCTION
270
10.1.2
OVERALL
ACTIVITY
OF
PDHC
BY
DISMUTATION
ASSAY
270
10.2
OC-OXOGLUTARATE
DEHYDROGENASE
COMPLEX
(OGDHC)
272
10.2.1
OVERALL
ACTIVITY
BY
NAD
+
REDUCTION
273
11
ASSAYS
FOR
OTHER
ENZYME
RELEVANT
PARAMETERS
275
11.1
SUBSTRATE
DETERMINATION
275
11.1.1
DETERMINATION
OF
NADP(H)
BY
ENZYMATIC
CYCLING
275
11.1.1.1
CYCLING
REACTION
276
11.1.2
DETERMINATION
OF
NAD(H)
BY
ENZYMATIC
CYCLING
277
11.2
PROTEIN
DETERMINATION
279
11.2.1
BIURET
ASSAY
279
XII
CONTENTS
11.2.2
BCA ASSAY
281
11.2.2.1
ASSAY
FOR
SOLUBLE
PROTEINS
281
11.2.2.2
MODIFICATION
FOR
IMMOBILIZED
PROTEINS
282
11.2.3
LOWRY
ASSAY
282
11.2.4
COOMASSIE
BINDING
ASSAY
(BRADFORD
ASSAY)
283
11.2.4.1
ASSAY
FOR
SOLUBLE
PROTEINS
284
11.2.4.2
MODIFICATION
FOR
IMMOBILIZED
PROTEINS
284
11.2.5
ABSORPTION
METHOD
285
11.2.6
FLUORIMETRIC
ASSAY
287
11.2.7
NINHYDRIN
ASSAY
288
11.2.7.1
NINHYDRIN
ASSAY
WITH
HYDROLYSIS
288
11.2.7.2
MODIFIED
NINHYDRIN
ASSAY
WITHOUT
HYDROLYSIS
289
11.2.8
PROTEIN
ASSAY
WITH
2
-
HYDROXY-
1-
NAPHTHALDEHYDE
290
GENERAL
LITERATURE
FOR
PROTEIN
ASSAYS
291
11.3
PHOSPHATE
DETERMINATION
291
11.4
DETERMINATION
OF
METAL
IONS
293
11.4.1
CALCIUM
AND
MAGNESIUM
293
11.4.2
IRON
294
11.4.2.1
DETERMINATION
WITH
FERROZINE
295
11.4.2.2
DETERMINATION
OF
FE
11
WITH
1,10-PHENANTHROLINE
IN
THE
PRESENCE
OF
FE
111
295
11.4.3
COPPER
296
11.4.3.1
BIQUINOLINE
METHOD
296
11.4.3.2
OXALYLDIHYDRAZIDE
METHOD
297
11.4.4
MANGANESE
297
11.4.4.1
COLORIMETRIC
ASSAY
298
11.4.4.2
ASSAY
WITH
L-(2-PYRIDYLAZO)-2-NAPHTHOL
(PAN)
298
11.4.5
ZINC
299
11.5
GLYCOPROTEIN
ASSAYS
300
11.5.1
IDENTIFICATION
IN
ELECTROPHORESIS
GELS
300
11.5.2
QUANTITATIVE
ANALYSIS
OF
PROTEIN-BOUND
HEXOSES
300
11.6
CROSS-LINKING
OF
PROTEINS
WITH
DIMETHYLSUBERIMIDATE
301
11.7
CONCENTRATING
ENZYME
SOLUTIONS
302
11.7.1
PRECIPITATION
303
11.7.2
ULTRAFILTRATION
AND
DIALYSIS
306
11.7.3
ULTRACENTRIFUGATION
307
11.7.4
LYOPHILIZATION
307
11.7.5
OTHER
CONCENTRATION METHODS
307
12
ENZYME
IMMUNOASSAYS
309
12.1
RADIOIMMUNOASSAYS
309
12.2
PRINCIPLE
OF
ENZYME
IMMUNOASSAYS
309
12.3
NONCOMPETITIVE
SOLID-PHASE
ENZYME
IMMUNOASSAY
311
12.4
COMPETITIVE
SOLID-PHASE
ENZYME
IMMUNOASSAY
312
12.5
METHODS
FOR
ENZYME
IMMUNOASSAYS
AND
IMMOBILIZATION
TECHNIQUES
312
12.5.1
PROTEIN
COUPLING
TO
CYANOGEN
BROMIDE
ACTIVATED AGAROSE
312
CONTENTS
XIII
12.5.2
COUPLING
OF
DIAMINOHEXYL
SPACER
313
12.5.3
PERIODATE
ACTIVATION
OF
CELLULOSE
314
12.5.4
INTRODUCTION
OF
THIOL
GROUPS
INTO
PROTEINS
(ANTIBODIES)
315
12.5.5
CONJUGATION
OF
A
PROTEIN
(ANTIBODY)
WITH
AN
ENZYME
(PEROXIDASE)
316
12.5.6
CONJUGATION
OF
B-GALACTOSIDASE
TO
PROTEINS
(ANTIBODIES)
BY
MBS
316
12.5.7
CONJUGATION
OF
ALKALINE
PHOSPHATASE
TO
ANTIBODIES
BY
GLUTARALDEHYDE
317
13
BINDING
MEASUREMENTS
319
13.1
DIFFERENT
TYPES
OF
BINDING
319
13.1.1
GENERAL
CONSIDERATIONS
319
13.1.2
HOW
CAN
SPECIFIC
REVERSIBLE
BINDING
BE
IDENTIFIED?
320
13.1.3
EXPERIMENTAL
ASPECTS
322
13.2
BINDING
MEASUREMENTS
BY
SIZE
DISCRIMINATION
325
13.2.1
EQUILIBRIUM
DIALYSIS
325
13.2.1.1
BINDING
OF
INDOLE
TO
BOVINE
SERUM
ALBUMIN
327
13.2.2
EVALUATION
OF
BINDING
EXPERIMENTS
329
13.2.3
ULTRAFILTRATION
330
13.2.4
GEL
FILTRATION
331
13.2.5
ULTRACENTRIFUGATION
332
13.3
SPECTROSCOPIC
METHODS
333
13.3.1
DIFFERENCE
SPECTROSCOPY
334
13.3.1.1
DIFFERENCE
SPECTROSCOPIC
TITRATION
OF
LIGANDS
BINDING
TO
CATALASE
336
13.3.1.2
EVALUATION
OF
SPECTROSCOPIC
BINDING
CURVES
339
13.3.2
FLUORESCENCE
SPECTROSCOPY
341
13.3.2.1
BINDING
OF
ANS
TO
BOVINE
SERUM
ALBUMIN
341
13.4
OTHER
BINDING
METHODS
344
13.4.1
RADIOACTIVE
LABELING
344
13.4.2
SURFACE
PLASMON
RESONANCE
(SPR)
345
14
ENZYMES
IN
TECHNICAL
APPLICATIONS
347
14.1
MODES
OF
ENZYME
IMMOBILIZATION
347
14.1.1
ADSORPTION
348
14.1.2
ENTRAPMENT
350
14.1.3
ENCAPSULATION
350
14.1.4
CROSS-LINKING
351
14.1.5
COVALENT
IMMOBILIZATION
TO
SOLID
SUPPORTS
351
14.1.5.1
SUPPORTS
351
14.1.5.2
SPACER
353
14.2
METHODS
FOR
ENZYME
IMMOBILIZATION
354
14.2.1
MICROENCAPSULATION
IN
NYLON
BEADS
355
14.2.2
ENTRAPMENT
IN
POLYACRYLAMIDE
355
14.2.3
COVALENT
IMMOBILIZATION
ON
GLASS
SURFACES
356
14.2.4
COVALENT
IMMOBILIZATION
ON
CONTROLLED-PORE
GLASS
(CPG)
358
14.2.5
COVALENT
IMMOBILIZATION TO
POLYAMIDE
360
XIV
CONTENTS
14.2.5.1
O-ALKYLATION
WITH
TRIETHYLOXONIUM
TETRAFLUOROBORATE
361
14.2.5.2
IMMOBILIZATION
TO
AMINO
GROUPS
AFTER
PARTIAL
HYDROLYSIS
OF
POLYAMIDE
363
14.2.5.3
IMMOBILIZATION
TO
CARBOXYL
GROUPS
AFTER
PARTIAL
HYDROLYSIS
OF
POLYAMIDE
364
14.2.6
IMMOBILIZATION
TO
POLYESTER
365
14.2.7
IMMOBILIZATION
BY
ALKALINE
HYDROLYSIS
AND
ACTIVATION
WITH
TOSYLCHLORIDE
367
14.2.8
ALKALINE
HYDROLYSIS
AND
ACTIVATION
BY
CARBONYLDIIMIDAZOL
368
14.3
ANALYSIS
OF
IMMOBILIZED
ENZYMES
368
14.3.1
GENERAL
PRINCIPLES
368
14.3.2
CONTINUOUS
PHOTOMETRIC
ASSAYS
FOR
IMMOBILIZED
ENZYMES
369
14.3.3
COFACTORS
IN
REACTIONS
WITH
IMMOBILIZED
ENZYMES
371
14.4
ENZYME
REACTORS
372
14.4.1
BATCH
REACTOR
(STIRRED-TANK
REACTOR)
373
14.4.2
MEMBRANE
REACTOR
373
14.4.3
SOLID-BED
REACTOR
374
14.4.4
IMMOBILIZED
CELLS
375
14.5
BIOSENSORS
375
14.5.1
ENZYME
ELECTRODES
375
14.5.2
IMMUNOELECTRODES
379
14.5.3
OTHER
BIOSENSORS
379
14.6
IMMOBILIZED
ENZYMES
IN
THERAPY
381
INDEX
383
|
| 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 | BV045943667 |
| classification_rvk | WC 4350 WD 5050 VK 8700 |
| classification_tum | CHE 828f |
| ctrlnum | (OCoLC)1083225456 (DE-599)DNB1175759481 |
| discipline | Chemie / Pharmazie Biologie Chemie |
| edition | Third edition |
| format | Book |
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| genre | (DE-588)4127380-1 Praktikum gnd-content |
| genre_facet | Praktikum |
| id | DE-604.BV045943667 |
| illustrated | Illustrated |
| indexdate | 2024-07-10T08:31:07Z |
| institution | BVB |
| isbn | 9783527346042 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-031325876 |
| oclc_num | 1083225456 |
| open_access_boolean | |
| owner | DE-29 DE-11 DE-91G DE-BY-TUM DE-19 DE-BY-UBM DE-703 DE-634 DE-355 DE-BY-UBR |
| owner_facet | DE-29 DE-11 DE-91G DE-BY-TUM DE-19 DE-BY-UBM DE-703 DE-634 DE-355 DE-BY-UBR |
| physical | xviii, 393 Seiten Illustrationen, Diagramme |
| publishDate | 2019 |
| publishDateSearch | 2019 |
| publishDateSort | 2019 |
| publisher | Wiley-VCH |
| record_format | marc |
| spelling | Bisswanger, Hans 1943- Verfasser (DE-588)129060461 aut Practical enzymology Hans Bisswanger Third edition Weinheim Wiley-VCH [2019] © 2019 xviii, 393 Seiten Illustrationen, Diagramme txt rdacontent n rdamedia nc rdacarrier Enzymkinetik (DE-588)4133166-7 gnd rswk-swf Enzym (DE-588)4014988-2 gnd rswk-swf Enzymtechnologie (DE-588)4135962-8 gnd rswk-swf Biochemie Biochemie u. Chemische Biologie Biochemistry Biowissenschaften Cellular & Molecular Medicine Chemie Chemistry Life Sciences Medical Science Medizin Zell- u. Molekularmedizin (DE-588)4127380-1 Praktikum 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 Erscheint auch als Online-Ausgabe, PDF 978-3-527-82081-8 Erscheint auch als Online-Ausgabe, EPUB 978-3-527-82080-1 Erscheint auch als Online-Ausgabe 978-3-527-82078-8 DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031325876&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 Enzymkinetik (DE-588)4133166-7 gnd Enzym (DE-588)4014988-2 gnd Enzymtechnologie (DE-588)4135962-8 gnd |
| subject_GND | (DE-588)4133166-7 (DE-588)4014988-2 (DE-588)4135962-8 (DE-588)4127380-1 |
| 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 | Enzymkinetik (DE-588)4133166-7 gnd Enzym (DE-588)4014988-2 gnd Enzymtechnologie (DE-588)4135962-8 gnd |
| topic_facet | Enzymkinetik Enzym Enzymtechnologie Praktikum |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=031325876&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT bisswangerhans practicalenzymology |