Principles and applications of fluorescence spectroscopy:
Saved in:
| Main Author: | |
|---|---|
| Format: | Book |
| Language: | English |
| Published: |
Oxford [u.a.]
Blackwell
2007
|
| Edition: | 1. publ. |
| Subjects: | |
| Online Access: | Inhaltsverzeichnis |
| Physical Description: | VIII, 255 S. Ill., graph. Darst. |
| ISBN: | 1405138912 9781405138918 |
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MARC
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| 020 | |a 9781405138918 |9 978-1-4051-3891-8 | ||
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| 100 | 1 | |a Albani, Jihad René |e Verfasser |4 aut | |
| 245 | 1 | 0 | |a Principles and applications of fluorescence spectroscopy |c Jihad René Albani |
| 250 | |a 1. publ. | ||
| 264 | 1 | |a Oxford [u.a.] |b Blackwell |c 2007 | |
| 300 | |a VIII, 255 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 650 | 4 | |a Biochemistry | |
| 650 | 4 | |a Fluorescence spectroscopy | |
| 650 | 4 | |a Spectrometry, Fluorescence | |
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Record in the Search Index
| _version_ | 1804137147912945664 |
|---|---|
| adam_text | 1 Absorption Spectroscopy Theory 1
1.1 Introduction 1
1.2 Characteristicsofan Absorption Spectrum 2
1.3 Beer Lambert Bouguer Law 4
1.4 Effectofthe Environment on Absorption Spectra 6
References 11
2 Determination of the Calcofluor White Molar Extinction Coefficient Value in
the Absence and Presence of ai Acid Glycoprotein 13
2.1 Introduction 13
2.2 Biological Material Used 13
2.2.1 Calcofluor White 13
2.2.2 a Acid glycoprotein 13
2.3 Experiments 16
2.3.1 Absorption spectrumof Calcofluor free in PBSbuffer 16
2.3.2 Determination of s value of Calcofluor White free in
PBS buffer 16
2.3.3 Determination of Calcofluor White £ value in the presence of
a i acid glycoprotein 16
2.4 Solution 17
References 19
3 Determination of Kinetic Parameters of Lactate Dehydrogenase 21
3.1 Objectiveof the Experiment 21
3.2 Absorption Spectrum ofNADH 21
3.3 Absorption Spectrum ofLDH 22
3.4 Enzymatic Activity ofLDH 22
3.5 Kinetic Parameters 22
3.6 Data and Results 22
3.6.1 Determination ofenzyme activity 23
3.6.2 Determination of kinetic parameters 23
3.7 Introduction to Kinetics and the Michaelis Menten Equation 26
3.7.1 Definitions 26
3.7.2 Reaction rates 26
References 32
4 Hydrolysis of p Nitrophenyl /J D Galactoside with /J Galactosidase
from E. coli 34
4.1 Introduction 34
4.2 Solutions to be Prepared 35
4.3 First day Experiments 35
4.3.1 Absorption spectrum of PNP 35
4.3.2 Absorption of PNP as a function of pH 36
4.3.3 InternalcalibrationofPNP 37
4.3.4 Determination ofjö galactosidase optimal pH 39
4.3.5 Determination of 0 galactosidase optimal temperature 40
4.4 Second day Experiments 40
4.4.1 Kinetics of p nitrophenyl ß D galactoside hydrolysis with
/J galactosidase 40
4.4.2 Determination of the ß galactosidase concentration in the test
tube 42
4.5 Third day Experiments
4.5.1 Determination ofKm and Vmax ofß galactosidase 44
4.5.2 Inhibiton of hydrolysis kinetics of p nitrophenyl ^ D galactoside 45
4.6 Fourth day Experiments
4.6.1 Effect of guanidine chloride concentration on ß galactosidase
activity
4.6.2 OD Variation with guanidine chloride
4.6.3 Mathematical derivation of Keq
4.6.4 Definition of the Standard Gibbs free energy, A Go/ 51
4.6.5 Relation between AGO/ and AG 51
4.6.6 Relation between AGO/ and K«, 52
4.6.7 Effect of guanidine chloride onhydrolysis kinetics of
p nitrophenyl /5 D galactoside
References
5 Starch Hydrolysis by Amylase 59
5.1 Objectives 59
59
5.2 Introduction
5.3 Materials 61
5.4 Procedures and Experiments
5.4.1 Preparation of a 20 g 1 ~ starch solution ,
5.4.2 Calibration curve for starch concentration „
5.4.3 Calibration curve for sugar concentration ,
5.4.4 Effect of pH jj
5.4.5 Temperature effect 69
5.4.6 Effect ofheat treatment at 90°C 70 i
5.4.7 Kinetics of starch hydrolysis *
5.4.8 Effect of inhibitor (Q1CI2) on the amylase activity 73
; 5.4.9 Effect of amylase concentration 73
; 5.4.10 Complement experiments that can be performed 77
5.4.11 Notes 77
References 78
6 Determination of the pKofa Dye 79
6.1 Definition ofpK 79
) 6.2 Spectrophotometric Determination ofpK 79
j 6.3 Determination of the pKof4 Methyl 2 Nitrophenol 81
I 6.3.1 Experimental procedure 81
J 6.3.2 Solution 83
| References 87
7 Fluorescence Spectroscopy Principles 88
7.1 Jablonski Diagram or Diagram of Electronic Transitions 88
4 7.2 Fluorescence Spectral Properties 91
j 7.2.1 General features 91
| 7.2.2 Stokesshift 93
7.2.3 Relationship between the emission spectrum and
| excitation wavelength 94
I 7.2.4 Inner filter effect 95
i 7.2.5 Fluorescence excitation spectrum 95
I 7.2.6 Mirror image rule 95
I 7.2.7 Fluorescence lifetime 96
j 7.2.8 Fluorescence quantum yield 101
j 7.2.9 Fluorescence and light diffusion 102
J 7.3 Fluorophore Structures and Properties 102
{ 7.3.1 Aromatic amino acids 104
! 7.3.2 Cofactors 108
I 7.3.3 Extrinsinc fluorophores 108
t 7.4 Polarity and Viscosity Effect on Quantum Yield and Emission Maximum
{ Position 111
I References 113
8 Effect of the St ructure and the Environment of a Fluorophore on
Its Absorption and Fluorescence Spectra 115
i Experiments 115
Questions 117
Answers 119
Reference 123
9 Fluorophore Characterization and Importance in Biology 124
9.1 Experiment 1. Quantitative Determination of Tryptophan in Proteins in
6MGuanidine 124
9.1.1 Introduction 124
9.1.2 Principle 124
9.1.3 Experiment 125
9.1.4 Results obtained with cytochrome Ö2 core 126
9.2 Experiment 2. Effect of the Inner Filter Effect on Fluorescence Data 127
9.2.1 Objectiveoftheexperiment 127
9.2.2 Experiment 127
9.2.3 Results 128
9.3 Experiment 3. Theoretical Spectral Resolution of Two Emitting
Fluorophores Within a Mixture 130
9.3.1 Objectiveoftheexperiment 130
9.3.2 Results 132
9.4 Experiment 4. Determination of Melting Temperature of Triglycerides in
Skimmed Milk Using Vitamin A Fluorescence 134
9.4.1 Introduction 134
9.4.2 Experiment to conduct 136
9.4.3 Results 136
References 138
10 Fluorescence Quenching 139
10.1 Introduction 139
10.2 Collisional Quenching: the Stern Volmer Relation 14°
10.3 Different Types of Dynamic Quenching 145
10.4 Static Quenching 147
10.4.1 Theory 147
10.5 Thermal Intensity Quenching 154
References 159
11 Fluorescence Polarization 160
11.1 Definition 160
11.2 Fluorescence Depolarization 162
11.2.1 Principles and applications l62
11.3 Fluorescence Anisotropy Decay Time 165
11.4 Depolarization and Energy Transfer 166
References 167
12 InteractionBetweenEthidiumBromideandDNA 168
12.1 Objectiveof the Experiment 168
12.2 DNA ExtractionfromCalfThymusor Herring Sperm 168
12.2.1 Destruction of cellular structure l
12.2.2 DNA extraction 168
12.2.3 DNA purification 169
12.2.4 Absorption spectrum of DNA 16q
12.3 Ethidium Bromide Titration with Herring DNA
12.4 Results Obtained with Herring DNA
12.4.1 Absorption and emission spectra
12.4.2 Analysis and interpretation of the results
12.5 Polarization Measurements 177
12.6 Results Obtained with Calf Thymus DNA 179
12.7 Temperature Effect on Fluorescence of the Ethidium Bromide DNA
Complex 180
References 182
13 Lens culinaris Agglutinin: Dynamics and Binding Studies 184
13.1 Experiment 1. Studies on the Accessibility of I~~ to a Fluorophore:
Quenching of Fluorescein Fluorescence with KI 184
¦ 13.1.1 Objectiveof the experiment 184
I 13.1.2 Experiment 184
| 13.1.3 Results 185
: 13.2 Experiment 2. Measurement of Rotational Correlation Time of
Fluorescein Bound to LCA with Polarization Studies 187
! 13.2.1 Objectiveof the work 187
. 13.2.2 Polarization studies as a function of temperature 187
13.2.3 Polarization studies as a function of sucrose at 20°C 187
13.2.4 Results 189
13.3 Experiment 3. Role of a L fucose in the Stability of
* Lectin Glycoproteins Complexes 190
13.3.1 Introduction 190
13.3.2 Binding studies 191
13.3.3 Results 192
References 196
j 14 Förster Energy Transfer 197
i 14.1 Principles and Applications 197
14.2 Energy transfer Parameters 202
1 14.3 Bioluminescence Resonance Energy Transfer 204
References 208
15 Binding ofTNSonBovine Serum Albumin at pH 3 and pH 7 210
15.1 Objectives 210
; 15.2 Experiments 210
I 15.2.1 Fluorescence emission spectra of TNS BSA at pH 3 and 7 210
15.2.2 Titration ofBSA with TNSat pH 3 and 7 210
15.2.3 Measurement of energy transfer efficiency from Trp residues
toTNS 211
j 15.2.4 Interaction between free Trp in solution and TNS 211
J 15.3 Results 211
1 16 Comet Test for Environmental Genotoxicity Evaluation: A Fluorescence
1 Microscopy Application 220
1 16.1 Principleofthe Comet Test 220
1 16.2 DNAStructure 220
1 16.3 DNA Reparation 221
16.4 Polycydic Aromatic Hydrocarbons 222
16.5 Reactive Oxygen Species 223
16.6 CausesofDNADamageandBiologicalConsequences 224
16.7 Typesof DNA Lesions 225
16.7.1 Induction of abasic sites, AP, apurinic, or apyrimidinic 225
16.7.2 Base modification 225
16.7.3 DNA adducts 225
16.7.4 Simple and double stranded breaks 225
16.8 PrincipleofFluorescenceMicroscopy 225
16.9 Comet Test 227
16.9.1 Experimental protocol 227
16.9.2 Nature of damage revealed with the Comet test 227
16.9.3 Advantages and limits of themethod 227
16.9.4 Result expression 231
References 231
17 Questions and Exercises 232
17.1 Questions 232
17.1.1 Questions with shorts answers 232
17.1.2 Find the error 232
17.1.3 Explain 233
17.1.4 Exercises 234
17.2 Solutions 241
17.2.1 Questions with short answers 241
17.2.2 Find the error 243
17.2.3 Explain 243
17.2.4 Exercises Solutions 2^
Index 253
Color plate appears between pages 168 and 169
|
| adam_txt |
1 Absorption Spectroscopy Theory 1
1.1 Introduction 1
1.2 Characteristicsofan Absorption Spectrum 2
1.3 Beer Lambert Bouguer Law 4
1.4 Effectofthe Environment on Absorption Spectra 6
References 11
2 Determination of the Calcofluor White Molar Extinction Coefficient Value in
the Absence and Presence of ai Acid Glycoprotein 13
2.1 Introduction 13
2.2 Biological Material Used 13
2.2.1 Calcofluor White 13
2.2.2 a\ Acid glycoprotein 13
2.3 Experiments 16
2.3.1 Absorption spectrumof Calcofluor free in PBSbuffer 16
2.3.2 Determination of s value of Calcofluor White free in
PBS buffer ' 16
2.3.3 Determination of Calcofluor White £ value in the presence of
a i acid glycoprotein 16
2.4 Solution 17
References 19
3 Determination of Kinetic Parameters of Lactate Dehydrogenase 21
3.1 Objectiveof the Experiment 21
3.2 Absorption Spectrum ofNADH 21
3.3 Absorption Spectrum ofLDH 22
3.4 Enzymatic Activity ofLDH 22
3.5 Kinetic Parameters 22
3.6 Data and Results 22
3.6.1 Determination ofenzyme activity 23
3.6.2 Determination of kinetic parameters 23
3.7 Introduction to Kinetics and the Michaelis Menten Equation 26
3.7.1 Definitions 26
3.7.2 Reaction rates 26
References 32
4 Hydrolysis of p Nitrophenyl /J D Galactoside with /J Galactosidase
from E. coli 34
4.1 Introduction 34
4.2 Solutions to be Prepared 35
4.3 First day Experiments 35
4.3.1 Absorption spectrum of PNP 35
4.3.2 Absorption of PNP as a function of pH 36
4.3.3 InternalcalibrationofPNP 37
4.3.4 Determination ofjö galactosidase optimal pH 39
4.3.5 Determination of 0 galactosidase optimal temperature 40
4.4 Second day Experiments 40
4.4.1 Kinetics of p nitrophenyl ß D galactoside hydrolysis with
/J galactosidase 40
4.4.2 Determination of the ß galactosidase concentration in the test
tube 42
4.5 Third day Experiments
4.5.1 Determination ofKm and Vmax ofß galactosidase 44
4.5.2 Inhibiton of hydrolysis kinetics of p nitrophenyl ^ D galactoside 45
4.6 Fourth day Experiments
4.6.1 Effect of guanidine chloride concentration on ß galactosidase
activity
4.6.2 OD Variation with guanidine chloride
4.6.3 Mathematical derivation of Keq
4.6.4 Definition of the Standard Gibbs free energy, A Go/ 51
4.6.5 Relation between AGO/ and AG' 51
4.6.6 Relation between AGO/ and K«, 52
4.6.7 Effect of guanidine chloride onhydrolysis kinetics of
p nitrophenyl /5 D galactoside
References
5 Starch Hydrolysis by Amylase 59
5.1 Objectives 59
59
5.2 Introduction
5.3 Materials 61
5.4 Procedures and Experiments
5.4.1 Preparation of a 20 g 1 ~' starch solution ,
5.4.2 Calibration curve for starch concentration „
5.4.3 Calibration curve for sugar concentration ,
5.4.4 Effect of pH jj
5.4.5 Temperature effect 69
5.4.6 Effect ofheat treatment at 90°C 70 i
5.4.7 Kinetics of starch hydrolysis *
5.4.8 Effect of inhibitor (Q1CI2) on the amylase activity 73
; 5.4.9 Effect of amylase concentration 73
'; 5.4.10 Complement experiments that can be performed 77
5.4.11 Notes 77
References 78
6 Determination of the pKofa Dye 79
6.1 Definition ofpK 79
) 6.2 Spectrophotometric Determination ofpK 79
j 6.3 Determination of the pKof4 Methyl 2 Nitrophenol 81
I 6.3.1 Experimental procedure 81
J 6.3.2 Solution 83
| References 87
7 Fluorescence Spectroscopy Principles 88
7.1 Jablonski Diagram or Diagram of Electronic Transitions 88
4 7.2 Fluorescence Spectral Properties 91
j 7.2.1 General features 91
| 7.2.2 Stokesshift 93
\ 7.2.3 Relationship between the emission spectrum and
| excitation wavelength 94
I 7.2.4 Inner filter effect 95
i 7.2.5 Fluorescence excitation spectrum 95
I 7.2.6 Mirror image rule 95
I 7.2.7 Fluorescence lifetime 96
j 7.2.8 Fluorescence quantum yield 101
j 7.2.9 Fluorescence and light diffusion 102
J 7.3 Fluorophore Structures and Properties 102
{ 7.3.1 Aromatic amino acids 104
! 7.3.2 Cofactors 108
I 7.3.3 Extrinsinc fluorophores 108
t 7.4 Polarity and Viscosity Effect on Quantum Yield and Emission Maximum
{ Position 111
I References 113
8 Effect of the St ructure and the Environment of a Fluorophore on
Its Absorption and Fluorescence Spectra 115
i Experiments 115
Questions 117
Answers 119
Reference 123
9 Fluorophore Characterization and Importance in Biology 124
9.1 Experiment 1. Quantitative Determination of Tryptophan in Proteins in
6MGuanidine 124
9.1.1 Introduction 124
9.1.2 Principle 124
9.1.3 Experiment 125
9.1.4 Results obtained with cytochrome Ö2 core 126
9.2 Experiment 2. Effect of the Inner Filter Effect on Fluorescence Data 127
9.2.1 Objectiveoftheexperiment 127
9.2.2 Experiment 127
9.2.3 Results 128
9.3 Experiment 3. Theoretical Spectral Resolution of Two Emitting
Fluorophores Within a Mixture 130
9.3.1 Objectiveoftheexperiment 130
9.3.2 Results 132
9.4 Experiment 4. Determination of Melting Temperature of Triglycerides in
Skimmed Milk Using Vitamin A Fluorescence 134
9.4.1 Introduction 134
9.4.2 Experiment to conduct 136
9.4.3 Results 136
References 138
10 Fluorescence Quenching 139
10.1 Introduction 139
10.2 Collisional Quenching: the Stern Volmer Relation 14°
10.3 Different Types of Dynamic Quenching 145
10.4 Static Quenching 147
10.4.1 Theory 147
10.5 Thermal Intensity Quenching 154
References 159
11 Fluorescence Polarization 160
11.1 Definition 160
11.2 Fluorescence Depolarization 162
11.2.1 Principles and applications l62
11.3 Fluorescence Anisotropy Decay Time 165
11.4 Depolarization and Energy Transfer 166
References 167
12 InteractionBetweenEthidiumBromideandDNA 168
12.1 Objectiveof the Experiment 168
12.2 DNA ExtractionfromCalfThymusor Herring Sperm 168
12.2.1 Destruction of cellular structure l
12.2.2 DNA extraction 168
12.2.3 DNA purification 169
12.2.4 Absorption spectrum of DNA 16q
12.3 Ethidium Bromide Titration with Herring DNA
12.4 Results Obtained with Herring DNA
12.4.1 Absorption and emission spectra
12.4.2 Analysis and interpretation of the results
12.5 Polarization Measurements 177
12.6 Results Obtained with Calf Thymus DNA 179
12.7 Temperature Effect on Fluorescence of the Ethidium Bromide DNA
Complex 180
References 182
13 Lens culinaris Agglutinin: Dynamics and Binding Studies 184
13.1 Experiment 1. Studies on the Accessibility of I~~ to a Fluorophore:
Quenching of Fluorescein Fluorescence with KI 184
'¦ 13.1.1 Objectiveof the experiment 184
I 13.1.2 Experiment 184
| 13.1.3 Results 185
: 13.2 Experiment 2. Measurement of Rotational Correlation Time of
\ Fluorescein Bound to LCA with Polarization Studies 187
! 13.2.1 Objectiveof the work 187
. 13.2.2 Polarization studies as a function of temperature 187
13.2.3 Polarization studies as a function of sucrose at 20°C 187
13.2.4 Results 189
13.3 Experiment 3. Role of a L fucose in the Stability of
* Lectin Glycoproteins Complexes 190
13.3.1 Introduction 190
13.3.2 Binding studies 191
13.3.3 Results 192
\ References 196
\
j 14 Förster Energy Transfer 197
i 14.1 Principles and Applications 197
14.2 Energy transfer Parameters 202
1 14.3 Bioluminescence Resonance Energy Transfer 204
References 208
15 Binding ofTNSonBovine Serum Albumin at pH 3 and pH 7 210
15.1 Objectives 210
; 15.2 Experiments 210
I 15.2.1 Fluorescence emission spectra of TNS BSA at pH 3 and 7 210
15.2.2 Titration ofBSA with TNSat pH 3 and 7 210
15.2.3 Measurement of energy transfer efficiency from Trp residues
toTNS 211
j 15.2.4 Interaction between free Trp in solution and TNS 211
J 15.3 Results 211
1 16 Comet Test for Environmental Genotoxicity Evaluation: A Fluorescence
1 Microscopy Application 220
1 16.1 Principleofthe Comet Test 220
1 16.2 DNAStructure 220
1 16.3 DNA Reparation 221
16.4 Polycydic Aromatic Hydrocarbons 222
16.5 Reactive Oxygen Species 223
16.6 CausesofDNADamageandBiologicalConsequences 224
16.7 Typesof DNA Lesions 225
16.7.1 Induction of abasic sites, AP, apurinic, or apyrimidinic 225
16.7.2 Base modification 225
16.7.3 DNA adducts 225
16.7.4 Simple and double stranded breaks 225
16.8 PrincipleofFluorescenceMicroscopy 225
16.9 Comet Test 227
16.9.1 Experimental protocol 227
16.9.2 Nature of damage revealed with the Comet test 227
16.9.3 Advantages and limits of themethod 227
16.9.4 Result expression 231
References 231
17 Questions and Exercises 232
17.1 Questions 232
17.1.1 Questions with shorts answers 232
17.1.2 Find the error 232
17.1.3 Explain 233
17.1.4 Exercises 234
17.2 Solutions 241
17.2.1 Questions with short answers 241
17.2.2 Find the error 243
17.2.3 Explain 243
17.2.4 Exercises Solutions 2^
Index 253
Color plate appears between pages 168 and 169 |
| any_adam_object | 1 |
| any_adam_object_boolean | 1 |
| author | Albani, Jihad René |
| author_facet | Albani, Jihad René |
| author_role | aut |
| author_sort | Albani, Jihad René |
| author_variant | j r a jr jra |
| building | Verbundindex |
| bvnumber | BV022883217 |
| callnumber-first | Q - Science |
| callnumber-label | QP519 |
| callnumber-raw | QP519.9.F56 |
| callnumber-search | QP519.9.F56 |
| callnumber-sort | QP 3519.9 F56 |
| callnumber-subject | QP - Physiology |
| classification_rvk | VG 8750 |
| classification_tum | CHE 808f CHE 243f |
| ctrlnum | (OCoLC)76939941 (DE-599)HBZHT015429893 |
| dewey-full | 543/.56 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 543 - Analytical chemistry |
| dewey-raw | 543/.56 |
| dewey-search | 543/.56 |
| dewey-sort | 3543 256 |
| dewey-tens | 540 - Chemistry and allied sciences |
| discipline | Chemie / Pharmazie Chemie |
| discipline_str_mv | Chemie / Pharmazie Chemie |
| edition | 1. publ. |
| format | Book |
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| id | DE-604.BV022883217 |
| illustrated | Illustrated |
| index_date | 2024-07-02T18:51:11Z |
| indexdate | 2024-07-09T21:07:41Z |
| institution | BVB |
| isbn | 1405138912 9781405138918 |
| language | English |
| lccn | 2006100265 |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-016088168 |
| oclc_num | 76939941 |
| open_access_boolean | |
| owner | DE-703 DE-91G DE-BY-TUM DE-29 DE-29T DE-19 DE-BY-UBM DE-634 DE-355 DE-BY-UBR |
| owner_facet | DE-703 DE-91G DE-BY-TUM DE-29 DE-29T DE-19 DE-BY-UBM DE-634 DE-355 DE-BY-UBR |
| physical | VIII, 255 S. Ill., graph. Darst. |
| publishDate | 2007 |
| publishDateSearch | 2007 |
| publishDateSort | 2007 |
| publisher | Blackwell |
| record_format | marc |
| spelling | Albani, Jihad René Verfasser aut Principles and applications of fluorescence spectroscopy Jihad René Albani 1. publ. Oxford [u.a.] Blackwell 2007 VIII, 255 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Biochemistry Fluorescence spectroscopy Spectrometry, Fluorescence Fluoreszenzspektroskopie (DE-588)4017701-4 gnd rswk-swf Biochemie (DE-588)4006777-4 gnd rswk-swf Fluoreszenzspektroskopie (DE-588)4017701-4 s DE-604 Biochemie (DE-588)4006777-4 s b DE-604 HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=016088168&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Albani, Jihad René Principles and applications of fluorescence spectroscopy Biochemistry Fluorescence spectroscopy Spectrometry, Fluorescence Fluoreszenzspektroskopie (DE-588)4017701-4 gnd Biochemie (DE-588)4006777-4 gnd |
| subject_GND | (DE-588)4017701-4 (DE-588)4006777-4 |
| title | Principles and applications of fluorescence spectroscopy |
| title_auth | Principles and applications of fluorescence spectroscopy |
| title_exact_search | Principles and applications of fluorescence spectroscopy |
| title_exact_search_txtP | Principles and applications of fluorescence spectroscopy |
| title_full | Principles and applications of fluorescence spectroscopy Jihad René Albani |
| title_fullStr | Principles and applications of fluorescence spectroscopy Jihad René Albani |
| title_full_unstemmed | Principles and applications of fluorescence spectroscopy Jihad René Albani |
| title_short | Principles and applications of fluorescence spectroscopy |
| title_sort | principles and applications of fluorescence spectroscopy |
| topic | Biochemistry Fluorescence spectroscopy Spectrometry, Fluorescence Fluoreszenzspektroskopie (DE-588)4017701-4 gnd Biochemie (DE-588)4006777-4 gnd |
| topic_facet | Biochemistry Fluorescence spectroscopy Spectrometry, Fluorescence Fluoreszenzspektroskopie Biochemie |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=016088168&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT albanijihadrene principlesandapplicationsoffluorescencespectroscopy |