Ultrasensitive and rapid enzyme immunoassay:
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
Amsterdam [u.a.]
Elsevier
1999
|
| Ausgabe: | 1. ed. |
| Schriftenreihe: | Laboratory techniques in biochemistry and molecular biology
27 |
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XVI, 334 S. Ill., graph. Darst. |
| ISBN: | 0444502017 0444502025 |
Internformat
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| 100 | 1 | |a Ishikawa, Eiji |e Verfasser |4 aut | |
| 245 | 1 | 0 | |a Ultrasensitive and rapid enzyme immunoassay |c Eiji Ishikawa |
| 250 | |a 1. ed. | ||
| 264 | 1 | |a Amsterdam [u.a.] |b Elsevier |c 1999 | |
| 300 | |a XVI, 334 S. |b Ill., graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 490 | 1 | |a Laboratory techniques in biochemistry and molecular biology |v 27 | |
| 650 | 7 | |a Radioimmunoassay |2 cabt | |
| 650 | 4 | |a Enzyme-linked immunosorbent assay - Laboratory manuals | |
| 650 | 7 | |a Technique immunoenzymatique |2 ram | |
| 650 | 4 | |a Enzyme-Linked Immunosorbent Assay | |
| 650 | 4 | |a Enzyme-linked immunosorbent assay |x Laboratory manuals | |
| 650 | 0 | 7 | |a Enzymimmunassay |0 (DE-588)4152477-9 |2 gnd |9 rswk-swf |
| 689 | 0 | 0 | |a Enzymimmunassay |0 (DE-588)4152477-9 |D s |
| 689 | 0 | |5 DE-604 | |
| 830 | 0 | |a Laboratory techniques in biochemistry and molecular biology |v 27 |w (DE-604)BV005871299 |9 27 | |
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Datensatz im Suchindex
| _version_ | 1804127617309212672 |
|---|---|
| adam_text | Contents
Preface v
Chapter 1. Introduction: classification of
immunoassays 1
Chapter 2. History of ultrasensitive
enzyme immunoassay 5
Chapter 3. Factors limiting the sensitivity of
noncompetitive heterogeneous solid
phase enzyme immunoassays 7
3.1. Factors limiting the sensitivity to antigens and antibodies 7
3.2. Factors limiting the sensitivity to antibodies 9
3.3. Factors limiting the sensitivity to antigens 14
Chapter 4. Methods to minimize effects of factors limiting
the sensitivity 17
4.1. Methods to minimize the nonspecific bindings of antigen and
antibody enzyme conjugates 17
4.1.1. Reducing the concentration of antigen and antibody
enzyme conjugates 17
4.1.2. Useof antibody fragments rather than intact antibodies 18
4.1.3. Hinge method for enzyme labeling of antibodies 21
4.1.4. Purification of antigen and antibody enzyme
conjugates 22
4.1.5. Addition of proteins analogous to antibodies and label
enzymes 24
4.1.6. Immune complex transfer from solid phase to solid
phase 25
vii
viii I
4.1.7. Miscellaneous conditions 25
4.2. Method for efficient trapping of antigens and antibodies 34
4.3. Methods using as full reactivities of antigens and antibodies as
possible 40
4.3.1. Indirect immobilization of antigens 40
4.3.2. Indirect immobilization of antibodies 53
4.3.3. Immunoreaction in solution and subsequent trapping on
a solid phase of the immune complex formed 54
4.4. Methods to reduce serum interference 64
4.4.1. Choice of enzyme labels 64
4.4.2. Use of high ionic concentrations 65
4.4.3. Indirect immobilization of antigens 66
4.4.4. Indirect immobilization of antibodies 75
4.4.5. Low concentrations of antigens and antibodies for
coating solid phases 76
4.4.6. Miscellaneous conditions 77
Chapter 5. Principle of the immune complex transfer
enzyme immunoassay 79
5.1. Immune complex transfer enzyme immunoassay of antibodies .. 79
5.2. Immune complex transfer enzyme immunoassays of antigens ... 91
5.3. Immune complex transfer enzyme immunoassay for simultaneous
detections of antigens and antibodies 93
Chapter 6. Potential of the immune complex transfer
enzyme immunoassay to improve the
sensitivity and its limitations 97
6.1. Improvement of sensitivity to antibodies 97
6.1.1. Immune complex transfer enzyme immunoassay I 98
6.1.2. Immune complex transfer enzyme immunoassay II .... 99
6.1.3. Immune complex transfer enzyme immunoassay III ... 103
6.1.4. Immune complex transfer enzyme immunoassay IV ... 104
6.1.5. Immune complex transfer enzyme immunoassay V 105
6.1.6. Immune complex transfer enzyme immunoassay VI ... 112 ]
6.1.7. Immune complex transfer enzyme immunoassay VII .. 114
6.1.8. Immune complex transfer enzyme immunoassay VIII .. 115 i
ix
6.2. Improvement of sensitivity to antigens 115
6.2.1. Immune complex transfer enzyme immunoassay IX ... 115
6.2.2. Immune complex transfer enzyme immunoassay X 118
6.3. Simultaneous detection of antigens and antibodies by the
immune complex transfer enzyme immunoassay 120
6.4. Further improvement of sensitivity 124
6.5. Assay variation 124
6.6. Factors limiting improvement in sensitivity of the immune
complex transfer enzyme immunoassay 125
6.6.1. Nonspecific adsorption and desorption of labeled
reactants 125
6.6.2. Direct contact of the first solid phase from which the
immune complex is eluted and the second solid phase to
which the immune complex is transferred 125
6.6.3. Affinities of antibodies used or measured 126
6.6.4. Detection limit of enzyme labels 128
6.6.5. Antibodies to enzyme labels 130
6.6.6. Antibodies to IgG from other species of animals 138
6.6.7. Unknown factors 138
Chapter 7. Ultrasensitive and rapid enzyme
immunoassay 141
7.1. Shaking for immunoreactions on solid phases 141
7.2. Use of larger sample volumes 147
7.3. Use of solid phases with larger surfaces 148
7.4. Use of circulating thin aqueous layers covering solid phase
surfaces 149
7.5. Advantages of circulating thin aqueous layer immunoassay 155
7.5.1. Rapid solid phase immunoassay 155
7.5.2. Saving of expensive reagents 155
7.5.3. Sensitive detection of label enzymes 155
7.6. Circulating thin aqueous layer immunoassay for antibodies 156
7.6.1. Immunoassay processes 156
7.6.2. Time courses of immunoreactions 158
7.6.3. Sensitivity 159
7.6.4. Advantages and disadvantages 163
7.6.5. Characteristics of different antibodies 165
X
7.7. Circulating thin aqueous layer immunoassay for antigens 170 j
7.7.1. Immunoassay processes 170
7.7.2. Time courses of immunoreactions 172 ;
7.7.3. Sensitivity 174 I
Chapter 8. Protocol of immune complex transfer enzyme ¦
immunoassay 177
8.1. Choice of enzymes as labels 177
8.2. Choice of enzyme labeling methods 177
8.3. Use of inactive forms of enzyme labels 178
8.4. Preparation of 2,4 dinitrophenyl bovine serum albumin for
immunization 178
8.5. Preparation of biotinyl and 2,4 dinitrophenyl bovine serum
albumin for immunoassays 179
8.6. Affinity purification of (anti 2,4 dinitrophenyl group) igG 181
8.7. Coating of solid phases with proteins 182
8.8. Preparations of 2,4 dinitrophenyl (biotinyl) antigens and
antibodies and antigen and antibody enzyme conjugates 182
8.9. Typical protocol of immune complex transfer enzyme
immunoassay V for antibody IgG 183
8.10. Typical protocols of immune complex transfer enzyme
immunoassays IX and X for antigens 187
Chapter 9. Ultrasensitive immunoassay for haptens .... 193
9.1. Introduction 193
9.2. Principle of noncompetitive (hetero two site) immunoassay 194
9.3. Feasibility of the principle 196
9.3.1. Method I using 2,4 dinitrophenyl anti peptide IgG and
avidin /i D galactosidase conjugate 196
9.3.2. Method II using streptavidin coated solid phase and anti
peptide Fab peroxidase conjugate 199
9.3.3. Method III by indirect biotinylation 202
9.3.4. Method IV 203 ,
9.4. Measurement of haptens in plasma and urine 205 ;
9.5. Other methods 210 I
I
xi
Chapter 10. Properties of the reagents for enzyme
labeling 211
10.1. Solubility 211
10.2. Stability and reactivity 212
10.3. Purity 221
Chapter 11. Enzyme labeling of antibodies 223
11.1. Introduction 223
11.2. Hinge method 225
11.3. Nonhinge method 231
11.4. Monomeric antibody enzyme conjugates 233
11.5. Affinity purified antibody enzyme conjugates 234
11.6. Microscale preparation of antibody enzyme conjugates 235
11.7. Characterization and evaluation of antibody enzyme conjugates 236
11.7.1. Molecular size 236
11.7.2. Purity 238
11.7.3. Yield 242
11.7.4. Stability 243
11.7.5. Specific and nonspecific bindings of antibody enzyme
conjugates 246
11.7.6. Comparison of the hinge method and the biotin avidin
method 247
Chapter 12. Preparation and affinity purification oflgG
fragments 249
12.1. Preparations of F(ab )2 and Fab 249
12.1.1. Pepsin digestion of IgG to F(ab )2 249
12.1.2. Reduction of F(ab )2 to Fab 250
12.1.3. Measurement of thiol groups in the Fab
preparation 252
12.1.4. Blocking thiol groups of Fab 252
12.2. Preparations of affinity purified IgG, F(ab )2 and Fab 253
12.2.1. Affinity purification of IgG 253
12.2.2. Affinity purification of F(ab )2 254
xii |
12.2.3. Direct affinity purifications of F(ab )2 and Fab from
antiserum 259
Chapter 13. Protocol for enzyme labeling of antibodies . 261
13.1. Introduction 261
13.2. Labeling of Fab with peroxidase by the hinge method using
maleimide derivatives 261
13.2.1. Preparation of 6 maleimidohexanoyl horseradish
peroxidase 261
13.2.2. Measurement of maleimide groups 262
13.2.3. Conjugation of Fab with 6 maleimidohexanoyl
peroxidase 263
13.3. Labeling of Fab with y8 D galactosidase by the hinge method
using maleimide derivatives 264
13.3.1. Introduction of maleimide groups into
/f D galactosidase 264
13.3.2. Conjugation of Fab with maleimide /i D
galactosidase 264
13.4. Labeling of Fab with alkaline phosphatase by the hinge
method using maleimide derivatives 265
13.4.1. Preparation of 6 maleimidohexanoyl alkaline
phosphatase 265
13.4.2. Conjugation of Fab with maleimide alkaline
phosphatase 266
13.5. Labeling of Fab with glucose 6 phosphate dehydrogenase by
the hinge method using maleimide derivatives 267
13.5.1. Introduction of maleimide groups into glucose
6 phosphate dehydrogenase 267
13.5.2. Conjugation of Fab with maleimide glucose
6 phosphate dehydrogenase 268
13.6. Labeling of IgG with /J D galactosidase by the hinge
method using maleimide derivatives 268
13.6.1. Reduction of IgG 268
13.6.2. Introduction of maleimide groups into
/8 D galactosidase 269
13.6.3. Conjugation of reduced IgG with maleimide
/J D galactosidase 269
i
xiii
13.7. Labeling of Fab with peroxidase by the hinge method
using pyridyl disulfide derivatives 270
13.7.1. Introduction of pyridyl disulfide groups into
peroxidase 270
13.7.2. Measurement of pyridyl disulfide groups 270
13.7.3. Conjugation of Fab with pyridyldisulfide
peroxidase 271
13.8. Nonhinge method 271
13.8.1. Conjugation of Fab with glutaraldehyde treated
peroxidase 271
13.8.2. Conjugation of Fab with periodate oxidized
peroxidase 272
13.8.3. Preparation of mercaptoacetyl IgG and F(ab )2 273
13.8.4. Conjugation of mercaptoacetyl IgG and F(ab )2 with
6 maleimidohexanoyl peroxidase 273
13.8.5. Conjugations of mercaptoacetyl IgG and F(ab )2
with 6 maleimidohexanoyl alkaline
phosphatase 274
Chapter 14. Protocol for labeling avidin with
2,4 dinitrophenyl groups and
j3 D galactosidase 277
14.1. Labeling of avidin with 2,4 dinitrophenyl groups 277
14.1.1. Preparation of mercaptoacetyl avidin 277
14.1.2. Preparation of a A 6 maleimidohexanoyl eA
2,4 dinitrophenyl L lysine 278
14.1.3. Conjugation ofaiV 6 maleimidohexanoyl e/V
2,4 dinitrophenyl L lysine with mercaptoacetyl
avidin 278
14.2. Labeling of avidin with 2,4 dinitrophenyl bovine serum
albumin 279
14.2.1. Preparation of mercaptoacetyl 2,4 dinitropheny 1
bovine serum albumin 279
14.2.2. Preparation of 6 maleimidohexanoyl avidin 279
14.2.3. Conjugation of 6 maleimidohexanoyl avidin
withmercaptoacetyl 2,4 dinitrophenyl bovine
serum albumin 280
xiv 1
14.3. Labeling of avidin with /i D galactosidase 281
Chapter 15. Enzyme labeling of antigens 283
Chapter 16. Protocol for enzyme labeling of antigens .. 289
16.1. Labeling of recombinant H1V 1 reverse transcriptase (rRT) with
2,4 dinitrophenyl groups 289
16.1.1. Preparation of mercaptoacetyl bovine serum
albumin 289 i
16.1.2. Preparation of a /V 6 maleimidohexanoyl e N
2,4 dinitrophenyl L lysine 290
16.1.3. Conjugation of 6 maleimidohexanoyI eJV 2,4 •
dinitrophenyl L lysine with mercaptoacetyl bovine
serum albumin 290
16.1.4. Preparation of 6 maleimidohexanoyl 2,4 dinitro
phenyl bovine serum albumin 290
16.1.5. Preparation of mercaptoacetyl rRT 291
16.1.6. Conjugation of mercaptoacetyl rRT to 6 maleimido
hexanoyl 2,4 dinitrophenyl bovine serum
albumin 292
16.2. Labeling of recombinant H1V 1 pl7 antigen (rpl7) with
2,4 dinitrophenyl groups 293
16.2.1. Preparation of mercaptoacetyl rp 17 293
16.2.2. Conjugation of mercaptoacetyl rp 17 with
6 maleimidohexanoyl 2,4 dinitrophenyl bovine
serum albumin 293
16.3. Labeling of recombinant HIV 1 p24 antigen (rp24) with
2,4 dinitrophenyl groups 295
16.3.1. Preparation of mercaptoacetyl rp24 295
16.3.2. Conjugation of mercaptoacetyl rp24 with
6 maleimidohexanoyl 2,4 dinitrophenyl bovine
serum albumin 295
16.4. Labeling of recombinant HIV 1 reverse transcriptase (rRT)
with /J D galactosidase: Method I 297
16.4.1. Preparation of maleimide ^ D galactosidase I 297
16.4.2. Conjugation of mercaptoacetyl rRT with
maleimide /S D galactosidase I 297
i
XV
16.5. Labeling of recombinant HIV 1 reverse transcriptase (rRT)
with ^ D galactosidase: Method II 298
16.5.1. Preparation of maleimide ^ D galactosidase II 298
16.5.2. Conjugation of mercaptoacetyl rRT with
maleimide /} D galactosidase II 298
16.6. Labeling of recombinant HIV 1 reverse transcriptase (rRT)
with /3 D galactosidase: Method III 299
16.6.1. Preparation of maleimide /} D galactosidase III 299
16.6.2. Conjugation of mercaptoacetyl rRT with
maleimide /3 D galactosidase III 300
16.7. Labeling of recombinant HIV 1 pl7 (rpl7) with
/3 D galactosidase 301
16.8. Labeling of recombinant HIV 1 p24 (rp24) with
/6 D galactosidase 301
Chapter 17. Assays of enzymes 303
17.1. Introduction 303
17.2. Assay of peroxidase 304
17.2.1. Colorimetric assay of peroxidase with
o phenylenediamine 304
17.2.2. Colorimetric assay of peroxidase with
3,3 ,5,5 tetramethylbenzidine 304
17.2.3. Fluorometric assay of peroxidase with
3 (4 hydroxyphenyl)propionic acid 305
17.3. Assay of/i D galactosidase 305
17.3.1. Colorimetric assay of /3 D galactosidase with
o nitrophenyl ^ D galactoside 305
17.3.2. Fluorometric assay of/6 D galactosidase with
4 methylumbelliferyl /6 D galactoside 306
17.4. Assay of alkaline phosphatase 306
17.4.1. Colorimetric assay of alkaline phosphatase with
p nitrophenylphosphate 306
17.4.2. Colorimetric assay of alkaline phosphatase by
enzymatic cycling 307
17.4.3. Fluorometric assay of alkaline phosphatase with
4 methylumbelliferyl phosphate 308
17.5. Assay of glucose 6 phosphate dehydrogenase 308
xvi
17.5.1. Bioluminescent assay of glucose 6 phosphate
dehydrogenase 308
References 311
Subject Index 327
|
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| id | DE-604.BV012927147 |
| illustrated | Illustrated |
| indexdate | 2024-07-09T18:36:12Z |
| institution | BVB |
| isbn | 0444502017 0444502025 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-008801351 |
| oclc_num | 40632809 |
| open_access_boolean | |
| owner | DE-703 DE-19 DE-BY-UBM DE-188 |
| owner_facet | DE-703 DE-19 DE-BY-UBM DE-188 |
| physical | XVI, 334 S. Ill., graph. Darst. |
| publishDate | 1999 |
| publishDateSearch | 1999 |
| publishDateSort | 1999 |
| publisher | Elsevier |
| record_format | marc |
| series | Laboratory techniques in biochemistry and molecular biology |
| series2 | Laboratory techniques in biochemistry and molecular biology |
| spelling | Ishikawa, Eiji Verfasser aut Ultrasensitive and rapid enzyme immunoassay Eiji Ishikawa 1. ed. Amsterdam [u.a.] Elsevier 1999 XVI, 334 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Laboratory techniques in biochemistry and molecular biology 27 Radioimmunoassay cabt Enzyme-linked immunosorbent assay - Laboratory manuals Technique immunoenzymatique ram Enzyme-Linked Immunosorbent Assay Enzyme-linked immunosorbent assay Laboratory manuals Enzymimmunassay (DE-588)4152477-9 gnd rswk-swf Enzymimmunassay (DE-588)4152477-9 s DE-604 Laboratory techniques in biochemistry and molecular biology 27 (DE-604)BV005871299 27 HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=008801351&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Ishikawa, Eiji Ultrasensitive and rapid enzyme immunoassay Laboratory techniques in biochemistry and molecular biology Radioimmunoassay cabt Enzyme-linked immunosorbent assay - Laboratory manuals Technique immunoenzymatique ram Enzyme-Linked Immunosorbent Assay Enzyme-linked immunosorbent assay Laboratory manuals Enzymimmunassay (DE-588)4152477-9 gnd |
| subject_GND | (DE-588)4152477-9 |
| title | Ultrasensitive and rapid enzyme immunoassay |
| title_auth | Ultrasensitive and rapid enzyme immunoassay |
| title_exact_search | Ultrasensitive and rapid enzyme immunoassay |
| title_full | Ultrasensitive and rapid enzyme immunoassay Eiji Ishikawa |
| title_fullStr | Ultrasensitive and rapid enzyme immunoassay Eiji Ishikawa |
| title_full_unstemmed | Ultrasensitive and rapid enzyme immunoassay Eiji Ishikawa |
| title_short | Ultrasensitive and rapid enzyme immunoassay |
| title_sort | ultrasensitive and rapid enzyme immunoassay |
| topic | Radioimmunoassay cabt Enzyme-linked immunosorbent assay - Laboratory manuals Technique immunoenzymatique ram Enzyme-Linked Immunosorbent Assay Enzyme-linked immunosorbent assay Laboratory manuals Enzymimmunassay (DE-588)4152477-9 gnd |
| topic_facet | Radioimmunoassay Enzyme-linked immunosorbent assay - Laboratory manuals Technique immunoenzymatique Enzyme-Linked Immunosorbent Assay Enzyme-linked immunosorbent assay Laboratory manuals Enzymimmunassay |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=008801351&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| volume_link | (DE-604)BV005871299 |
| work_keys_str_mv | AT ishikawaeiji ultrasensitiveandrapidenzymeimmunoassay |