ZA200503475B - Non-competetive immunoassay for small analytes - Google Patents
Non-competetive immunoassay for small analytes Download PDFInfo
- Publication number
- ZA200503475B ZA200503475B ZA200503475A ZA200503475A ZA200503475B ZA 200503475 B ZA200503475 B ZA 200503475B ZA 200503475 A ZA200503475 A ZA 200503475A ZA 200503475 A ZA200503475 A ZA 200503475A ZA 200503475 B ZA200503475 B ZA 200503475B
- Authority
- ZA
- South Africa
- Prior art keywords
- binding partner
- analyte
- seq
- binding
- binds
- Prior art date
Links
- 238000003018 immunoassay Methods 0.000 title description 19
- 230000027455 binding Effects 0.000 claims abstract description 146
- 238000009739 binding Methods 0.000 claims abstract description 146
- 239000012491 analyte Substances 0.000 claims abstract description 65
- 230000036963 noncompetitive effect Effects 0.000 claims abstract description 30
- 238000002967 competitive immunoassay Methods 0.000 claims abstract description 26
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 14
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims abstract description 13
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims abstract description 13
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 10
- BQJCRHHNABKAKU-KBQPJGBKSA-N morphine Chemical compound O([C@H]1[C@H](C=C[C@H]23)O)C4=C5[C@@]12CCN(C)[C@@H]3CC5=CC=C4O BQJCRHHNABKAKU-KBQPJGBKSA-N 0.000 claims description 90
- 229960005181 morphine Drugs 0.000 claims description 54
- 239000003153 chemical reaction reagent Substances 0.000 claims description 29
- 238000003556 assay Methods 0.000 claims description 28
- 150000001413 amino acids Chemical class 0.000 claims description 20
- 238000002823 phage display Methods 0.000 claims description 17
- 229940079593 drug Drugs 0.000 claims description 15
- 239000003814 drug Substances 0.000 claims description 15
- 239000003446 ligand Substances 0.000 claims description 15
- 238000012360 testing method Methods 0.000 claims description 15
- 229960004242 dronabinol Drugs 0.000 claims description 13
- 238000002866 fluorescence resonance energy transfer Methods 0.000 claims description 13
- CYQFCXCEBYINGO-UHFFFAOYSA-N THC Natural products C1=C(C)CCC2C(C)(C)OC3=CC(CCCCC)=CC(O)=C3C21 CYQFCXCEBYINGO-UHFFFAOYSA-N 0.000 claims description 12
- CYQFCXCEBYINGO-IAGOWNOFSA-N delta1-THC Chemical compound C1=C(C)CC[C@H]2C(C)(C)OC3=CC(CCCCC)=CC(O)=C3[C@@H]21 CYQFCXCEBYINGO-IAGOWNOFSA-N 0.000 claims description 12
- 238000000034 method Methods 0.000 claims description 9
- 102000014914 Carrier Proteins Human genes 0.000 claims description 8
- 108091008324 binding proteins Proteins 0.000 claims description 8
- 230000008569 process Effects 0.000 claims description 6
- KWTSXDURSIMDCE-QMMMGPOBSA-N (S)-amphetamine Chemical compound C[C@H](N)CC1=CC=CC=C1 KWTSXDURSIMDCE-QMMMGPOBSA-N 0.000 claims description 4
- 229940025084 amphetamine Drugs 0.000 claims description 4
- 238000004519 manufacturing process Methods 0.000 claims description 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 23
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 15
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 15
- OROGSEYTTFOCAN-DNJOTXNNSA-N codeine Chemical compound C([C@H]1[C@H](N(CC[C@@]112)C)C3)=C[C@H](O)[C@@H]1OC1=C2C3=CC=C1OC OROGSEYTTFOCAN-DNJOTXNNSA-N 0.000 description 14
- 239000012634 fragment Substances 0.000 description 14
- 108020004414 DNA Proteins 0.000 description 12
- 238000002372 labelling Methods 0.000 description 12
- 210000002700 urine Anatomy 0.000 description 12
- 238000011534 incubation Methods 0.000 description 11
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- XQYZDYMELSJDRZ-UHFFFAOYSA-N papaverine Chemical compound C1=C(OC)C(OC)=CC=C1CC1=NC=CC2=CC(OC)=C(OC)C=C12 XQYZDYMELSJDRZ-UHFFFAOYSA-N 0.000 description 10
- 210000003296 saliva Anatomy 0.000 description 10
- 238000002965 ELISA Methods 0.000 description 9
- 241000588724 Escherichia coli Species 0.000 description 8
- 229910052693 Europium Inorganic materials 0.000 description 8
- OGPBJKLSAFTDLK-UHFFFAOYSA-N europium atom Chemical compound [Eu] OGPBJKLSAFTDLK-UHFFFAOYSA-N 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- GVGLGOZIDCSQPN-PVHGPHFFSA-N Heroin Chemical compound O([C@H]1[C@H](C=C[C@H]23)OC(C)=O)C4=C5[C@@]12CCN(C)[C@@H]3CC5=CC=C4OC(C)=O GVGLGOZIDCSQPN-PVHGPHFFSA-N 0.000 description 7
- 239000000427 antigen Substances 0.000 description 7
- 102000036639 antigens Human genes 0.000 description 7
- 108091007433 antigens Proteins 0.000 description 7
- 239000000872 buffer Substances 0.000 description 7
- 229960004126 codeine Drugs 0.000 description 7
- 230000009260 cross reactivity Effects 0.000 description 7
- 229960002069 diamorphine Drugs 0.000 description 7
- OROGSEYTTFOCAN-UHFFFAOYSA-N hydrocodone Natural products C1C(N(CCC234)C)C2C=CC(O)C3OC2=C4C1=CC=C2OC OROGSEYTTFOCAN-UHFFFAOYSA-N 0.000 description 7
- 238000004091 panning Methods 0.000 description 7
- 239000013612 plasmid Substances 0.000 description 7
- 230000035945 sensitivity Effects 0.000 description 7
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 6
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 6
- 229960003669 carbenicillin Drugs 0.000 description 6
- FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- 230000014509 gene expression Effects 0.000 description 6
- 238000002649 immunization Methods 0.000 description 6
- 238000000746 purification Methods 0.000 description 6
- 239000013598 vector Substances 0.000 description 6
- AKNNEGZIBPJZJG-MSOLQXFVSA-N (-)-noscapine Chemical compound CN1CCC2=CC=3OCOC=3C(OC)=C2[C@@H]1[C@@H]1C2=CC=C(OC)C(OC)=C2C(=O)O1 AKNNEGZIBPJZJG-MSOLQXFVSA-N 0.000 description 5
- 229930008281 A03AD01 - Papaverine Natural products 0.000 description 5
- 241000894006 Bacteria Species 0.000 description 5
- 239000004098 Tetracycline Substances 0.000 description 5
- 239000007983 Tris buffer Substances 0.000 description 5
- AKNNEGZIBPJZJG-UHFFFAOYSA-N alpha-noscapine Natural products CN1CCC2=CC=3OCOC=3C(OC)=C2C1C1C2=CC=C(OC)C(OC)=C2C(=O)O1 AKNNEGZIBPJZJG-UHFFFAOYSA-N 0.000 description 5
- 239000011324 bead Substances 0.000 description 5
- 230000002860 competitive effect Effects 0.000 description 5
- 108020004999 messenger RNA Proteins 0.000 description 5
- PLPRGLOFPNJOTN-UHFFFAOYSA-N narcotine Natural products COc1ccc2C(OC(=O)c2c1OC)C3Cc4c(CN3C)cc5OCOc5c4OC PLPRGLOFPNJOTN-UHFFFAOYSA-N 0.000 description 5
- 229960004708 noscapine Drugs 0.000 description 5
- 229960001789 papaverine Drugs 0.000 description 5
- 229960002180 tetracycline Drugs 0.000 description 5
- 229930101283 tetracycline Natural products 0.000 description 5
- 235000019364 tetracycline Nutrition 0.000 description 5
- 238000002877 time resolved fluorescence resonance energy transfer Methods 0.000 description 5
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 4
- 239000011543 agarose gel Substances 0.000 description 4
- 239000007853 buffer solution Substances 0.000 description 4
- 239000013522 chelant Substances 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 150000003522 tetracyclines Chemical class 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 238000012875 competitive assay Methods 0.000 description 3
- 238000004520 electroporation Methods 0.000 description 3
- 239000013604 expression vector Substances 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000010187 selection method Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 201000009032 substance abuse Diseases 0.000 description 3
- 231100000027 toxicology Toxicity 0.000 description 3
- 238000000844 transformation Methods 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 2
- 229920000742 Cotton Polymers 0.000 description 2
- 101100224495 Drosophila melanogaster Chrac-14 gene Proteins 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 2
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000012411 cloning technique Methods 0.000 description 2
- ZPUCINDJVBIVPJ-LJISPDSOSA-N cocaine Chemical compound O([C@H]1C[C@@H]2CC[C@@H](N2C)[C@H]1C(=O)OC)C(=O)C1=CC=CC=C1 ZPUCINDJVBIVPJ-LJISPDSOSA-N 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- KAKKHKRHCKCAGH-UHFFFAOYSA-L disodium;(4-nitrophenyl) phosphate;hexahydrate Chemical compound O.O.O.O.O.O.[Na+].[Na+].[O-][N+](=O)C1=CC=C(OP([O-])([O-])=O)C=C1 KAKKHKRHCKCAGH-UHFFFAOYSA-L 0.000 description 2
- 239000002359 drug metabolite Substances 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 230000008014 freezing Effects 0.000 description 2
- 238000007710 freezing Methods 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 238000001597 immobilized metal affinity chromatography Methods 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- 229960000318 kanamycin Drugs 0.000 description 2
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 238000010257 thawing Methods 0.000 description 2
- CUKWUWBLQQDQAC-VEQWQPCFSA-N (3s)-3-amino-4-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2s,3s)-1-[[(2s)-1-[(2s)-2-[[(1s)-1-carboxyethyl]carbamoyl]pyrrolidin-1-yl]-3-(1h-imidazol-5-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-methyl-1-ox Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C1=CC=C(O)C=C1 CUKWUWBLQQDQAC-VEQWQPCFSA-N 0.000 description 1
- XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 1
- USSIQXCVUWKGNF-UHFFFAOYSA-N 6-(dimethylamino)-4,4-diphenylheptan-3-one Chemical compound C=1C=CC=CC=1C(CC(C)N(C)C)(C(=O)CC)C1=CC=CC=C1 USSIQXCVUWKGNF-UHFFFAOYSA-N 0.000 description 1
- ITZMJCSORYKOSI-AJNGGQMLSA-N APGPR Enterostatin Chemical compound C[C@H](N)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N1[C@H](C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)CCC1 ITZMJCSORYKOSI-AJNGGQMLSA-N 0.000 description 1
- 102000005862 Angiotensin II Human genes 0.000 description 1
- 101800000733 Angiotensin-2 Proteins 0.000 description 1
- 101710132601 Capsid protein Proteins 0.000 description 1
- 101710094648 Coat protein Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- LTMHDMANZUZIPE-AMTYYWEZSA-N Digoxin Natural products O([C@H]1[C@H](C)O[C@H](O[C@@H]2C[C@@H]3[C@@](C)([C@@H]4[C@H]([C@]5(O)[C@](C)([C@H](O)C4)[C@H](C4=CC(=O)OC4)CC5)CC3)CC2)C[C@@H]1O)[C@H]1O[C@H](C)[C@@H](O[C@H]2O[C@@H](C)[C@H](O)[C@@H](O)C2)[C@@H](O)C1 LTMHDMANZUZIPE-AMTYYWEZSA-N 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- VAYOSLLFUXYJDT-RDTXWAMCSA-N Lysergic acid diethylamide Chemical compound C1=CC(C=2[C@H](N(C)C[C@@H](C=2)C(=O)N(CC)CC)C2)=C3C2=CNC3=C1 VAYOSLLFUXYJDT-RDTXWAMCSA-N 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- JEYCTXHKTXCGPB-UHFFFAOYSA-N Methaqualone Chemical compound CC1=CC=CC=C1N1C(=O)C2=CC=CC=C2N=C1C JEYCTXHKTXCGPB-UHFFFAOYSA-N 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 101710141454 Nucleoprotein Proteins 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 101710083689 Probable capsid protein Proteins 0.000 description 1
- 238000002123 RNA extraction Methods 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 229940123445 Tricyclic antidepressant Drugs 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000000862 absorption spectrum Methods 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 229950006323 angiotensin ii Drugs 0.000 description 1
- 229940046545 animal allergen extract Drugs 0.000 description 1
- 230000003302 anti-idiotype Effects 0.000 description 1
- 238000003149 assay kit Methods 0.000 description 1
- 229940125717 barbiturate Drugs 0.000 description 1
- 229940049706 benzodiazepine Drugs 0.000 description 1
- 150000001557 benzodiazepines Chemical class 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 229930003827 cannabinoid Natural products 0.000 description 1
- 239000003557 cannabinoid Substances 0.000 description 1
- 229940065144 cannabinoids Drugs 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 229960003920 cocaine Drugs 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- XLMALTXPSGQGBX-GCJKJVERSA-N dextropropoxyphene Chemical compound C([C@](OC(=O)CC)([C@H](C)CN(C)C)C=1C=CC=CC=1)C1=CC=CC=C1 XLMALTXPSGQGBX-GCJKJVERSA-N 0.000 description 1
- 229960004193 dextropropoxyphene Drugs 0.000 description 1
- LTMHDMANZUZIPE-PUGKRICDSA-N digoxin Chemical compound C1[C@H](O)[C@H](O)[C@@H](C)O[C@H]1O[C@@H]1[C@@H](C)O[C@@H](O[C@@H]2[C@H](O[C@@H](O[C@@H]3C[C@@H]4[C@]([C@@H]5[C@H]([C@]6(CC[C@@H]([C@@]6(C)[C@H](O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)C[C@@H]2O)C)C[C@@H]1O LTMHDMANZUZIPE-PUGKRICDSA-N 0.000 description 1
- 229960005156 digoxin Drugs 0.000 description 1
- LTMHDMANZUZIPE-UHFFFAOYSA-N digoxine Natural products C1C(O)C(O)C(C)OC1OC1C(C)OC(OC2C(OC(OC3CC4C(C5C(C6(CCC(C6(C)C(O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)CC2O)C)CC1O LTMHDMANZUZIPE-UHFFFAOYSA-N 0.000 description 1
- 239000003344 environmental pollutant Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000002189 fluorescence spectrum Methods 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000000383 hazardous chemical Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 229950002454 lysergide Drugs 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000003340 mental effect Effects 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229960001797 methadone Drugs 0.000 description 1
- 229960002803 methaqualone Drugs 0.000 description 1
- 238000002493 microarray Methods 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000007483 microbial process Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 229940127240 opiate Drugs 0.000 description 1
- -1 pH 7.8 Chemical compound 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- JTJMJGYZQZDUJJ-UHFFFAOYSA-N phencyclidine Chemical compound C1CCCCN1C1(C=2C=CC=CC=2)CCCCC1 JTJMJGYZQZDUJJ-UHFFFAOYSA-N 0.000 description 1
- 229950010883 phencyclidine Drugs 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 239000012898 sample dilution Substances 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 150000003431 steroids Chemical class 0.000 description 1
- 231100000736 substance abuse Toxicity 0.000 description 1
- 208000011117 substance-related disease Diseases 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- OFVLGDICTFRJMM-WESIUVDSSA-N tetracycline Chemical compound C1=CC=C2[C@](O)(C)[C@H]3C[C@H]4[C@H](N(C)C)C(O)=C(C(N)=O)C(=O)[C@@]4(O)C(O)=C3C(=O)C2=C1O OFVLGDICTFRJMM-WESIUVDSSA-N 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 231100000167 toxic agent Toxicity 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 239000003029 tricyclic antidepressant agent Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/44—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material not provided for elsewhere, e.g. haptens, metals, DNA, RNA, amino acids
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/94—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving narcotics or drugs or pharmaceuticals, neurotransmitters or associated receptors
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/536—Immunoassay; Biospecific binding assay; Materials therefor with immune complex formed in liquid phase
- G01N33/542—Immunoassay; Biospecific binding assay; Materials therefor with immune complex formed in liquid phase with steric inhibition or signal modification, e.g. fluorescent quenching
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
- G01N33/6857—Antibody fragments
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/94—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving narcotics or drugs or pharmaceuticals, neurotransmitters or associated receptors
- G01N33/946—CNS-stimulants, e.g. cocaine, amphetamines
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/94—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving narcotics or drugs or pharmaceuticals, neurotransmitters or associated receptors
- G01N33/948—Sedatives, e.g. cannabinoids, barbiturates
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/94—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving narcotics or drugs or pharmaceuticals, neurotransmitters or associated receptors
- G01N33/9486—Analgesics, e.g. opiates, aspirine
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2470/00—Immunochemical assays or immunoassays characterised by the reaction format or reaction type
- G01N2470/04—Sandwich assay format
- G01N2470/06—Second binding partner specifically binding complex of analyte with first binding partner
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Hematology (AREA)
- Biomedical Technology (AREA)
- Urology & Nephrology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Physics & Mathematics (AREA)
- Food Science & Technology (AREA)
- Biotechnology (AREA)
- Analytical Chemistry (AREA)
- Microbiology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Cell Biology (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Organic Chemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Anesthesiology (AREA)
- Emergency Medicine (AREA)
- Pain & Pain Management (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Investigating Or Analysing Materials By The Use Of Chemical Reactions (AREA)
- Wrappers (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FI20022048A FI20022048A0 (fi) | 2002-11-18 | 2002-11-18 | Ei-kompetetiivinen immunomääritys pienille analyyteille |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ZA200503475B true ZA200503475B (en) | 2006-07-26 |
Family
ID=8564953
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ZA200503475A ZA200503475B (en) | 2002-11-18 | 2005-04-29 | Non-competetive immunoassay for small analytes |
Country Status (17)
| Country | Link |
|---|---|
| US (1) | US7749712B2 (da) |
| EP (1) | EP1579222B8 (da) |
| JP (1) | JP4729701B2 (da) |
| CN (1) | CN1711476B (da) |
| AT (1) | ATE408146T1 (da) |
| BR (1) | BRPI0316384B8 (da) |
| CA (1) | CA2503509C (da) |
| DE (1) | DE60323538D1 (da) |
| DK (1) | DK1579222T3 (da) |
| EA (1) | EA200500643A1 (da) |
| ES (1) | ES2312828T3 (da) |
| FI (1) | FI20022048A0 (da) |
| MX (1) | MXPA05005288A (da) |
| NO (1) | NO338417B1 (da) |
| NZ (1) | NZ539714A (da) |
| WO (1) | WO2004046733A1 (da) |
| ZA (1) | ZA200503475B (da) |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030109067A1 (en) | 2001-12-06 | 2003-06-12 | Immunetech, Inc. | Homogeneous immunoassays for multiple allergens |
| JP2007040834A (ja) * | 2005-08-03 | 2007-02-15 | Japan Science & Technology Agency | 免疫測定用試薬 |
| FI20075251A0 (fi) | 2007-04-13 | 2007-04-13 | Hytest Oy | Immunomääritys epästabiilien antigeenien määrittämiseksi |
| GB0707870D0 (en) * | 2007-04-23 | 2007-05-30 | Selected Antibodies Ltd | Assay Devices and Methods and Components for use Therein |
| EP2223122B1 (en) * | 2007-12-18 | 2011-08-31 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Endogenous morphine or a naturally occuring metabolite thereof as a marker for sepsis |
| GB0725234D0 (en) * | 2007-12-24 | 2008-02-06 | Oxtex Ltd | Electrochemical assays |
| ES2443065T3 (es) * | 2008-04-02 | 2014-02-17 | Vivacta Limited | Un método para detectar una sustancia química |
| US8093018B2 (en) | 2008-05-20 | 2012-01-10 | Otsuka Pharmaceutical Co., Ltd. | Antibody identifying an antigen-bound antibody and an antigen-unbound antibody, and method for preparing the same |
| FI20085579A0 (fi) * | 2008-06-12 | 2008-06-12 | Valtion Teknillinen | Kannabiskäytön toteaminen |
| DE102008049601A1 (de) * | 2008-09-30 | 2010-04-01 | Siemens Healthcare Diagnostics Products Gmbh | Antikörper zur Bestimmung des Prothrombin-Fragments F2/F1+2 in einem homogenen Immunoassay |
| MX2011003927A (es) | 2009-07-21 | 2011-07-20 | Sekisui Medical Co Ltd | Metodo de medicion de insulina. |
| WO2011053783A2 (en) * | 2009-10-30 | 2011-05-05 | Merck Sharp & Dohme Corp. | Ax213 and ax132 pcsk9 antagonists and variants |
| CA2780845C (en) * | 2009-11-19 | 2014-12-30 | Proteinexpress Co., Ltd. | Fluoroimmunoassay method |
| US8883978B2 (en) | 2010-05-11 | 2014-11-11 | Institute For Cancer Research | Antibodies to tumor endothelial marker 7R |
| US9599608B2 (en) * | 2011-09-21 | 2017-03-21 | Fujirebio Inc. | Antibody against affinity complex |
| AU2012325697B2 (en) * | 2011-10-21 | 2015-11-26 | Decimadx, Llc | Point-of care immunoassay for quantitative small analyte detection |
| EP2637021A1 (de) | 2012-03-06 | 2013-09-11 | Securetec Detektions-Systeme AG | Verfahren und Vorrichtung zum Nachweis von Analyten |
| US9804161B1 (en) | 2012-05-14 | 2017-10-31 | Lawrence Livermore National Security, Llc | Detector and related, devices, methods and systems |
| EP2722669A1 (de) | 2012-10-22 | 2014-04-23 | Securetec Detektions-Systeme AG | Verfahren und Vorrichtung zum Nachweis von illegalen Drogen |
| JP6673895B2 (ja) | 2014-03-21 | 2020-03-25 | エスティー アンド ティー インターナショナル，インコーポレイティド | アサ属抽出方法及び組成物 |
| FI126746B (en) | 2014-04-07 | 2017-05-15 | Teknologian Tutkimuskeskus Vtt Oy | Antibody to HT-2 toxin-HT-2 toxin antibody complex |
| WO2017053567A1 (en) * | 2015-09-22 | 2017-03-30 | Delta Tm Technologies | Designing customized protein-specific buffer systems |
| CA3002903A1 (en) | 2015-10-23 | 2017-04-27 | Fred Hutchinson Cancer Research Center | Methods to create chemically-induced dimerizing protein systems for regulation of cellular events |
| CN108779169B (zh) * | 2015-12-21 | 2022-06-07 | 图尔库大学 | 针对包含蓝细菌环肽肝毒素的免疫复合物的抗体 |
| AU2017209523A1 (en) * | 2016-01-22 | 2018-08-09 | Affimedix, Inc. | Device for detection of vitamin D metabolites |
| AU2017301763B2 (en) * | 2016-07-29 | 2023-07-06 | Diazyme Laboratories, Inc. | Methods and compositions for assaying vitamin D |
| IL294218A (en) | 2019-12-27 | 2022-08-01 | Chiome Bioscience Inc | Antibody against cdcp1 |
| CN116963779A (zh) | 2020-09-02 | 2023-10-27 | 国立大学法人东京大学 | 癌症免疫微环境的调节物质及其预防、诊断或治疗 |
| CA3239740A1 (en) * | 2021-12-03 | 2023-06-08 | Tim C. LEUTKENS | High selective cd229 antigen binding domains and methods of use |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3996345A (en) * | 1974-08-12 | 1976-12-07 | Syva Company | Fluorescence quenching with immunological pairs in immunoassays |
| US5223441A (en) | 1986-10-09 | 1993-06-29 | Syntex (U.S.A.) Inc. | Receptors for immune complexes |
| EP0759976A4 (en) | 1994-03-30 | 2001-02-07 | Igen Int Inc | THE INSULATION AND PRODUCTION OF CATALYTIC ANTIBODIES USING PHAGENTECHNOLOGY |
| JP3025633B2 (ja) | 1995-12-05 | 2000-03-27 | 株式会社蛋白工学研究所 | グルタチオン結合活性を有するポリペプチド及びその製造方法 |
| JP4228095B2 (ja) * | 1999-12-17 | 2009-02-25 | 東ソー株式会社 | 免疫測定方法および免疫測定試薬 |
| CN1136450C (zh) * | 2000-11-03 | 2004-01-28 | 厦门大学 | 具有荧光共振能量转移特征的成对蛋白及其用途 |
-
2002
- 2002-11-18 FI FI20022048A patent/FI20022048A0/fi unknown
-
2003
- 2003-11-17 ES ES03773761T patent/ES2312828T3/es not_active Expired - Lifetime
- 2003-11-17 CN CN2003801034664A patent/CN1711476B/zh not_active Expired - Lifetime
- 2003-11-17 NZ NZ539714A patent/NZ539714A/en not_active IP Right Cessation
- 2003-11-17 CA CA2503509A patent/CA2503509C/en not_active Expired - Lifetime
- 2003-11-17 EP EP03773761A patent/EP1579222B8/en not_active Expired - Lifetime
- 2003-11-17 MX MXPA05005288A patent/MXPA05005288A/es active IP Right Grant
- 2003-11-17 AT AT03773761T patent/ATE408146T1/de not_active IP Right Cessation
- 2003-11-17 DK DK03773761T patent/DK1579222T3/da active
- 2003-11-17 DE DE60323538T patent/DE60323538D1/de not_active Expired - Lifetime
- 2003-11-17 JP JP2004552756A patent/JP4729701B2/ja not_active Expired - Lifetime
- 2003-11-17 WO PCT/FI2003/000875 patent/WO2004046733A1/en active IP Right Grant
- 2003-11-17 EA EA200500643A patent/EA200500643A1/ru unknown
- 2003-11-17 US US10/535,260 patent/US7749712B2/en active Active
- 2003-11-17 BR BRPI0316384A patent/BRPI0316384B8/pt active IP Right Grant
-
2005
- 2005-04-29 ZA ZA200503475A patent/ZA200503475B/en unknown
- 2005-06-13 NO NO20052849A patent/NO338417B1/no not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| FI20022048A0 (fi) | 2002-11-18 |
| JP2006506634A (ja) | 2006-02-23 |
| US7749712B2 (en) | 2010-07-06 |
| EP1579222B1 (en) | 2008-09-10 |
| ES2312828T3 (es) | 2009-03-01 |
| NZ539714A (en) | 2007-03-30 |
| BRPI0316384B1 (pt) | 2016-07-05 |
| NO338417B1 (no) | 2016-08-15 |
| BRPI0316384B8 (pt) | 2021-07-27 |
| AU2003282143A1 (en) | 2004-06-15 |
| CN1711476B (zh) | 2010-09-08 |
| WO2004046733A1 (en) | 2004-06-03 |
| CN1711476A (zh) | 2005-12-21 |
| ATE408146T1 (de) | 2008-09-15 |
| BR0316384A (pt) | 2005-10-04 |
| MXPA05005288A (es) | 2005-08-16 |
| CA2503509C (en) | 2013-02-05 |
| EP1579222A1 (en) | 2005-09-28 |
| NO20052849L (no) | 2005-06-13 |
| CA2503509A1 (en) | 2004-06-03 |
| US20060246506A1 (en) | 2006-11-02 |
| JP4729701B2 (ja) | 2011-07-20 |
| DE60323538D1 (de) | 2008-10-23 |
| DK1579222T3 (da) | 2008-11-17 |
| EA200500643A1 (ru) | 2005-12-29 |
| EP1579222B8 (en) | 2009-01-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2503509C (en) | Non-competitive immunoassay for small analytes | |
| US8518653B2 (en) | Detection of cannabis use | |
| US8802382B2 (en) | Cobalamin assay | |
| AU2003282143B2 (en) | Non-competitive immunoassay for small analytes | |
| EP3129403B1 (en) | Antibody against ht-2 toxin-ht-2 toxin antibody complex |