NO329866B1 - Fremgangsmate for pavisning av nativt N-terminalt proBNP i en prove som utfores i "sandwich"-format ved anvendelse av minst to antistoffer som gjenkjenner forskjellige epitoper i det native N-terminale proBNP, og som samtidig kan bindes til nativt N-terminalt proBNP, anvendelse av fremgangsmaten for differensiering mellom prover, anvendelse av rekombinant N-terminalt proBNP som standard i en fremgangsmate, antistoffer mot N-terminalt proBNP fremstilt ved immunisering av en egnet organisme med rekombinant fremstilt N-terminalt proBNP, samt cellelinje. - Google Patents
Fremgangsmate for pavisning av nativt N-terminalt proBNP i en prove som utfores i "sandwich"-format ved anvendelse av minst to antistoffer som gjenkjenner forskjellige epitoper i det native N-terminale proBNP, og som samtidig kan bindes til nativt N-terminalt proBNP, anvendelse av fremgangsmaten for differensiering mellom prover, anvendelse av rekombinant N-terminalt proBNP som standard i en fremgangsmate, antistoffer mot N-terminalt proBNP fremstilt ved immunisering av en egnet organisme med rekombinant fremstilt N-terminalt proBNP, samt cellelinje. Download PDFInfo
- Publication number
- NO329866B1 NO329866B1 NO20013698A NO20013698A NO329866B1 NO 329866 B1 NO329866 B1 NO 329866B1 NO 20013698 A NO20013698 A NO 20013698A NO 20013698 A NO20013698 A NO 20013698A NO 329866 B1 NO329866 B1 NO 329866B1
- Authority
- NO
- Norway
- Prior art keywords
- terminal probnp
- antibodies
- probnp
- terminal
- native
- Prior art date
Links
- 108010008064 pro-brain natriuretic peptide (1-76) Proteins 0.000 title claims abstract description 147
- 238000000034 method Methods 0.000 title claims abstract description 53
- 230000003053 immunization Effects 0.000 title claims description 28
- 230000004069 differentiation Effects 0.000 title claims description 14
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 30
- 238000001514 detection method Methods 0.000 claims description 27
- 238000002649 immunization Methods 0.000 claims description 27
- 150000001413 amino acids Chemical class 0.000 claims description 22
- 206010019280 Heart failures Diseases 0.000 claims description 17
- 238000004519 manufacturing process Methods 0.000 claims description 16
- 230000009257 reactivity Effects 0.000 claims description 10
- 238000000746 purification Methods 0.000 claims description 5
- 238000002955 isolation Methods 0.000 claims description 2
- 210000002700 urine Anatomy 0.000 claims description 2
- 238000012216 screening Methods 0.000 claims 1
- 102400001263 NT-proBNP Human genes 0.000 abstract description 19
- 101800000407 Brain natriuretic peptide 32 Proteins 0.000 abstract description 11
- 102400000667 Brain natriuretic peptide 32 Human genes 0.000 abstract description 11
- 101800002247 Brain natriuretic peptide 45 Proteins 0.000 abstract description 11
- HPNRHPKXQZSDFX-OAQDCNSJSA-N nesiritide Chemical compound C([C@H]1C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CO)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1N=CNC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 HPNRHPKXQZSDFX-OAQDCNSJSA-N 0.000 abstract description 11
- 101800001904 NT-proBNP Proteins 0.000 abstract description 2
- 239000000523 sample Substances 0.000 description 29
- 238000004458 analytical method Methods 0.000 description 24
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 22
- 238000009739 binding Methods 0.000 description 19
- 230000027455 binding Effects 0.000 description 18
- 235000001014 amino acid Nutrition 0.000 description 17
- 238000006243 chemical reaction Methods 0.000 description 17
- 102000004196 processed proteins & peptides Human genes 0.000 description 15
- 239000000243 solution Substances 0.000 description 14
- 101710187802 Natriuretic peptides B Proteins 0.000 description 13
- 108090000623 proteins and genes Proteins 0.000 description 13
- 230000009870 specific binding Effects 0.000 description 13
- 102100036836 Natriuretic peptides B Human genes 0.000 description 12
- 210000002381 plasma Anatomy 0.000 description 12
- 239000007790 solid phase Substances 0.000 description 12
- 239000012491 analyte Substances 0.000 description 11
- 238000011534 incubation Methods 0.000 description 11
- 230000035945 sensitivity Effects 0.000 description 11
- 210000002966 serum Anatomy 0.000 description 11
- 239000011780 sodium chloride Substances 0.000 description 11
- 210000004027 cell Anatomy 0.000 description 10
- 239000002953 phosphate buffered saline Substances 0.000 description 10
- 239000000872 buffer Substances 0.000 description 9
- 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 8
- 210000004369 blood Anatomy 0.000 description 8
- 239000008280 blood Substances 0.000 description 8
- 239000000427 antigen Substances 0.000 description 7
- 102000036639 antigens Human genes 0.000 description 7
- 108091007433 antigens Proteins 0.000 description 7
- 239000011534 wash buffer Substances 0.000 description 7
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 6
- 241000699670 Mus sp. Species 0.000 description 6
- 102000003992 Peroxidases Human genes 0.000 description 6
- 108010090804 Streptavidin Proteins 0.000 description 6
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 6
- 108040007629 peroxidase activity proteins Proteins 0.000 description 6
- 238000005406 washing Methods 0.000 description 6
- 101800001288 Atrial natriuretic factor Proteins 0.000 description 5
- 102400001282 Atrial natriuretic peptide Human genes 0.000 description 5
- 101800001890 Atrial natriuretic peptide Proteins 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 5
- 241000588724 Escherichia coli Species 0.000 description 5
- 229960002685 biotin Drugs 0.000 description 5
- 239000011616 biotin Substances 0.000 description 5
- NSQLIUXCMFBZME-MPVJKSABSA-N carperitide Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 NSQLIUXCMFBZME-MPVJKSABSA-N 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 239000011159 matrix material Substances 0.000 description 5
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 241001494479 Pecora Species 0.000 description 4
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 4
- 235000020958 biotin Nutrition 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 230000001900 immune effect Effects 0.000 description 4
- 239000003550 marker Substances 0.000 description 4
- 238000005259 measurement Methods 0.000 description 4
- 239000002243 precursor Substances 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 238000003786 synthesis reaction Methods 0.000 description 4
- 239000013598 vector Substances 0.000 description 4
- 206010003445 Ascites Diseases 0.000 description 3
- SHIBSTMRCDJXLN-UHFFFAOYSA-N Digoxigenin Natural products C1CC(C2C(C3(C)CCC(O)CC3CC2)CC2O)(O)C2(C)C1C1=CC(=O)OC1 SHIBSTMRCDJXLN-UHFFFAOYSA-N 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 3
- 230000008033 biological extinction Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 239000011248 coating agent Substances 0.000 description 3
- 238000000576 coating method Methods 0.000 description 3
- 230000002860 competitive effect Effects 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- QONQRTHLHBTMGP-UHFFFAOYSA-N digitoxigenin Natural products CC12CCC(C3(CCC(O)CC3CC3)C)C3C11OC1CC2C1=CC(=O)OC1 QONQRTHLHBTMGP-UHFFFAOYSA-N 0.000 description 3
- SHIBSTMRCDJXLN-KCZCNTNESA-N digoxigenin Chemical compound C1([C@@H]2[C@@]3([C@@](CC2)(O)[C@H]2[C@@H]([C@@]4(C)CC[C@H](O)C[C@H]4CC2)C[C@H]3O)C)=CC(=O)OC1 SHIBSTMRCDJXLN-KCZCNTNESA-N 0.000 description 3
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 239000005556 hormone Substances 0.000 description 3
- 229940088597 hormone Drugs 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 238000003018 immunoassay Methods 0.000 description 3
- 238000002372 labelling Methods 0.000 description 3
- 239000007791 liquid phase Substances 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 239000013610 patient sample Substances 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 235000018102 proteins Nutrition 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 108090001008 Avidin Proteins 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 2
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 102100034296 Natriuretic peptides A Human genes 0.000 description 2
- 101710187800 Natriuretic peptides A Proteins 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- UIIMBOGNXHQVGW-DEQYMQKBSA-M Sodium bicarbonate-14C Chemical compound [Na+].O[14C]([O-])=O UIIMBOGNXHQVGW-DEQYMQKBSA-M 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 238000002820 assay format Methods 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000012875 competitive assay Methods 0.000 description 2
- 239000007857 degradation product Substances 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- -1 haptens Proteins 0.000 description 2
- 210000004754 hybrid cell Anatomy 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 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 2
- 239000007788 liquid Substances 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 239000006249 magnetic particle Substances 0.000 description 2
- 230000004060 metabolic process Effects 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 229920003023 plastic Polymers 0.000 description 2
- 238000003752 polymerase chain reaction Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- XOJVVFBFDXDTEG-UHFFFAOYSA-N pristane Chemical compound CC(C)CCCC(C)CCCC(C)CCCC(C)C XOJVVFBFDXDTEG-UHFFFAOYSA-N 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 238000011896 sensitive detection Methods 0.000 description 2
- 229910000029 sodium carbonate Inorganic materials 0.000 description 2
- 239000010421 standard material Substances 0.000 description 2
- WPLOVIFNBMNBPD-ATHMIXSHSA-N subtilin Chemical compound CC1SCC(NC2=O)C(=O)NC(CC(N)=O)C(=O)NC(C(=O)NC(CCCCN)C(=O)NC(C(C)CC)C(=O)NC(=C)C(=O)NC(CCCCN)C(O)=O)CSC(C)C2NC(=O)C(CC(C)C)NC(=O)C1NC(=O)C(CCC(N)=O)NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C1NC(=O)C(=C/C)/NC(=O)C(CCC(N)=O)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C2NC(=O)CNC(=O)C3CCCN3C(=O)C(NC(=O)C3NC(=O)C(CC(C)C)NC(=O)C(=C)NC(=O)C(CCC(O)=O)NC(=O)C(NC(=O)C(CCCCN)NC(=O)C(N)CC=4C5=CC=CC=C5NC=4)CSC3)C(C)SC2)C(C)C)C(C)SC1)CC1=CC=CC=C1 WPLOVIFNBMNBPD-ATHMIXSHSA-N 0.000 description 2
- IKALWTASUOCXGQ-ZWAPJTDOSA-N 7-[(3aS,4S,6aR)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-2-amino-2-butyl-3-oxoheptanoic acid 1-hydroxypyrrolidine-2,5-dione Chemical class ON1C(CCC1=O)=O.C(CCCC[C@@H]1SC[C@@H]2NC(=O)N[C@H]12)(=O)C(C(=O)O)(CCCC)N IKALWTASUOCXGQ-ZWAPJTDOSA-N 0.000 description 1
- 239000005541 ACE inhibitor Substances 0.000 description 1
- 101800004616 Adrenomedullin Proteins 0.000 description 1
- 102400001318 Adrenomedullin Human genes 0.000 description 1
- 229910002012 Aerosil® Inorganic materials 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- FGUUSXIOTUKUDN-IBGZPJMESA-N C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 Chemical compound C1(=CC=CC=C1)N1C2=C(NC([C@H](C1)NC=1OC(=NN=1)C1=CC=CC=C1)=O)C=CC=C2 FGUUSXIOTUKUDN-IBGZPJMESA-N 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 229920002271 DEAE-Sepharose Polymers 0.000 description 1
- 102000002045 Endothelin Human genes 0.000 description 1
- 108050009340 Endothelin Proteins 0.000 description 1
- 208000013875 Heart injury Diseases 0.000 description 1
- 101500026735 Homo sapiens Brain natriuretic peptide 32 Proteins 0.000 description 1
- 101000928278 Homo sapiens Natriuretic peptides B Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 241001625930 Luria Species 0.000 description 1
- 101710151321 Melanostatin Proteins 0.000 description 1
- CERQOIWHTDAKMF-UHFFFAOYSA-M Methacrylate Chemical compound CC(=C)C([O-])=O CERQOIWHTDAKMF-UHFFFAOYSA-M 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 102400000064 Neuropeptide Y Human genes 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 206010030113 Oedema Diseases 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 239000012614 Q-Sepharose Substances 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 210000000683 abdominal cavity Anatomy 0.000 description 1
- ULCUCJFASIJEOE-NPECTJMMSA-N adrenomedullin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)NCC(=O)N[C@@H]1C(N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CSSC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)[C@@H](C)O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCSC)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 ULCUCJFASIJEOE-NPECTJMMSA-N 0.000 description 1
- 230000000274 adsorptive effect Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 239000001166 ammonium sulphate Substances 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 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 1
- 229940044094 angiotensin-converting-enzyme inhibitor Drugs 0.000 description 1
- 230000001745 anti-biotin effect Effects 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 230000006287 biotinylation Effects 0.000 description 1
- 238000007413 biotinylation Methods 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 230000000747 cardiac effect Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 208000029078 coronary artery disease Diseases 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000005786 degenerative changes Effects 0.000 description 1
- 230000015961 delipidation Effects 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 238000013399 early diagnosis Methods 0.000 description 1
- 230000002526 effect on cardiovascular system Effects 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 239000012149 elution buffer Substances 0.000 description 1
- ZUBDGKVDJUIMQQ-UBFCDGJISA-N endothelin-1 Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(O)=O)NC(=O)[C@H]1NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@@H](CC=2C=CC(O)=CC=2)NC(=O)[C@H](C(C)C)NC(=O)[C@H]2CSSC[C@@H](C(N[C@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N2)=O)NC(=O)[C@@H](CO)NC(=O)[C@H](N)CSSC1)C1=CNC=N1 ZUBDGKVDJUIMQQ-UBFCDGJISA-N 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229930182470 glycoside Natural products 0.000 description 1
- 150000002338 glycosides Chemical class 0.000 description 1
- 210000001308 heart ventricle Anatomy 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 230000003054 hormonal effect Effects 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 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 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 230000003907 kidney function Effects 0.000 description 1
- 239000004816 latex Substances 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 210000004165 myocardium Anatomy 0.000 description 1
- 239000000692 natriuretic peptide Substances 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- URPYMXQQVHTUDU-OFGSCBOVSA-N nucleopeptide y Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 URPYMXQQVHTUDU-OFGSCBOVSA-N 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 230000037081 physical activity Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 235000019260 propionic acid Nutrition 0.000 description 1
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 239000013074 reference sample Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000029058 respiratory gaseous exchange Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000013214 routine measurement Methods 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 238000012106 screening analysis Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 229940043517 specific immunoglobulins Drugs 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 229940124549 vasodilator Drugs 0.000 description 1
- 239000003071 vasodilator agent Substances 0.000 description 1
- 230000003313 weakening effect Effects 0.000 description 1
Classifications
-
- 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
-
- 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
- G01N33/6887—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids from muscle, cartilage or connective tissue
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/26—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against hormones ; against hormone releasing or inhibiting factors
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Organic Chemistry (AREA)
- Pathology (AREA)
- Analytical Chemistry (AREA)
- Cell Biology (AREA)
- General Physics & Mathematics (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Endocrinology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Seasonings (AREA)
- Measurement Of Velocity Or Position Using Acoustic Or Ultrasonic Waves (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Saccharide Compounds (AREA)
- Measurement Of Radiation (AREA)
- Analysing Materials By The Use Of Radiation (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE19903489 | 1999-01-29 | ||
DE19911044 | 1999-03-12 | ||
PCT/EP2000/000602 WO2000045176A2 (de) | 1999-01-29 | 2000-01-27 | VERFAHREN ZUM NACHWEIS VON N-TERMINALEM proBNP |
Publications (3)
Publication Number | Publication Date |
---|---|
NO20013698D0 NO20013698D0 (no) | 2001-07-27 |
NO20013698L NO20013698L (no) | 2001-09-28 |
NO329866B1 true NO329866B1 (no) | 2011-01-17 |
Family
ID=26051550
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO20013698A NO329866B1 (no) | 1999-01-29 | 2001-07-27 | Fremgangsmate for pavisning av nativt N-terminalt proBNP i en prove som utfores i "sandwich"-format ved anvendelse av minst to antistoffer som gjenkjenner forskjellige epitoper i det native N-terminale proBNP, og som samtidig kan bindes til nativt N-terminalt proBNP, anvendelse av fremgangsmaten for differensiering mellom prover, anvendelse av rekombinant N-terminalt proBNP som standard i en fremgangsmate, antistoffer mot N-terminalt proBNP fremstilt ved immunisering av en egnet organisme med rekombinant fremstilt N-terminalt proBNP, samt cellelinje. |
Country Status (21)
Country | Link |
---|---|
US (1) | US20070059767A1 (pl) |
EP (2) | EP1698901B1 (pl) |
JP (1) | JP3987284B2 (pl) |
KR (1) | KR100572542B1 (pl) |
CN (2) | CN101046478B (pl) |
AT (2) | ATE373826T1 (pl) |
AU (1) | AU758562B2 (pl) |
CA (1) | CA2359667C (pl) |
CY (1) | CY1108450T1 (pl) |
DE (2) | DE50014666D1 (pl) |
DK (2) | DK1151304T3 (pl) |
ES (2) | ES2312062T3 (pl) |
HU (1) | HU228625B1 (pl) |
IL (2) | IL144062A0 (pl) |
NO (1) | NO329866B1 (pl) |
NZ (1) | NZ512762A (pl) |
PL (1) | PL204235B1 (pl) |
PT (1) | PT1698901E (pl) |
RU (1) | RU2218568C2 (pl) |
WO (1) | WO2000045176A2 (pl) |
ZA (1) | ZA200106193B (pl) |
Families Citing this family (35)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
MXPA03004105A (es) | 2002-05-14 | 2004-10-15 | Hoffmann La Roche | Elaboracion de una prognosis en casos de enfermedad cardiaca usando una combinacion de marcadores. |
GB0216191D0 (en) * | 2002-07-11 | 2002-08-21 | Univ Leicester | Plasma urotensin in human heart failure |
FR2843396B1 (fr) * | 2002-08-07 | 2005-04-15 | Bio Rad Pasteur | Anticorps specifiques pour le diagnostic de l'insuffisance cardiaque |
US20050287613A1 (en) * | 2002-11-18 | 2005-12-29 | George Jackowski | Polyclonal-polyclonal ELISA assay for detecting N-terminus-proBNP |
US20040096919A1 (en) * | 2002-11-18 | 2004-05-20 | Michelle Davey | Polyclonal-monoclonal ELISA assay for detecting N-terminus proBNP |
US6960472B2 (en) * | 2002-11-18 | 2005-11-01 | Ottawa Heart Institute Research Corporation | Monoclonal antibodies against N-Terminus proBNP |
JP4610025B2 (ja) * | 2002-11-18 | 2011-01-12 | シン.クス ファーマ、インコーポレイテッド | NT−proBNP検出用ポリクローナル・モノクローナル・エライサ検定法 |
EP1562984B1 (de) * | 2002-11-20 | 2006-08-09 | B.R.A.H.M.S Aktiengesellschaft | Sandwich-immunoassay zur bestimmung von proanp-teilpeptiden |
US7767419B2 (en) * | 2003-02-04 | 2010-08-03 | Nexus Dx, Inc. | Calibrator for NT-proBNP immunoassay |
DK1625163T3 (da) | 2003-05-12 | 2011-12-05 | Hoffmann La Roche | Fremgangsmåde til at påvise proBNP med en monoklonal antistofbinding til aminosyrerne 38-43 |
GB2403533A (en) | 2003-06-30 | 2005-01-05 | Orion Corp | Atrial natriuretic peptide and brain natriuretic peptide and assays and uses thereof |
EP1522857A1 (en) * | 2003-10-09 | 2005-04-13 | Universiteit Maastricht | Method for identifying a subject at risk of developing heart failure by determining the level of galectin-3 or thrombospondin-2 |
DE10355731A1 (de) | 2003-11-28 | 2005-06-30 | Roche Diagnostics Gmbh | Analytischer Sandwichtest zur Bestimmung von NT-proBNP |
GB0329288D0 (en) | 2003-12-18 | 2004-01-21 | Inverness Medical Switzerland | Monitoring method and apparatus |
AT500800B1 (de) * | 2004-09-08 | 2008-07-15 | Biomedica Medizinprodukte Gmbh | Verfahren zur bestimmung von probnp |
FR2863269B1 (fr) * | 2005-01-14 | 2006-05-26 | Bio Rad Pasteur | Peptides specifiques pour le diagnostic de l'insuffisance cardiaque |
DE102005003687A1 (de) * | 2005-01-26 | 2006-07-27 | Sphingo Tec Gmbh | Immunoassay zur Bestimmung der Freisetzung von Neurotensin in die Zirkulation |
EP1722232A1 (en) * | 2005-05-09 | 2006-11-15 | F.Hoffmann-La Roche Ag | Devices and methods for diagnosing or predicting early stage cardiac dysfunctions |
EP1909207B1 (de) * | 2006-09-11 | 2015-03-04 | F.Hoffmann-La Roche Ag | Messbereichserweiterung chromatografischer Schnellteste |
EP1909206A1 (de) * | 2006-09-11 | 2008-04-09 | Roche Diagnostics GmbH | Messbereichserweiterung chromatografischer Schnellteste |
DE102006060835A1 (de) * | 2006-12-22 | 2008-06-26 | Brahms Aktiengesellschaft | Diagnose und Risikostratifizierung des akuten Koronarsyndroms mittels CT-proET-1 in Kombination mit NT-proBNP |
WO2008089994A1 (en) * | 2007-01-25 | 2008-07-31 | Roche Diagnostics Gmbh | Use of igfbp-7 in the assessment of heart failure |
EP1970709B1 (en) * | 2007-03-06 | 2013-07-10 | Roche Diagnostics GmbH | The use of BNP-type peptides for predicting the need for dialysis |
CA2680339C (en) | 2007-03-08 | 2017-02-28 | F. Hoffmann-La Roche Ag | Use of slim-1 in the assessment of heart failure |
EP2195660A1 (en) * | 2007-08-30 | 2010-06-16 | Roche Diagnostics GmbH | Means and methods for the discrimination of gdf-15 elevation related or unrelated to cardiac disorders |
EP2274622B1 (en) | 2008-04-30 | 2014-10-08 | The Governing Council of the University of Toronto | Use of sfrp-3 in the assessment of heart failure |
CN102549436A (zh) | 2009-07-27 | 2012-07-04 | 霍夫曼-拉罗奇有限公司 | mimecan在评价心力衰竭中的用途 |
CN102549429B (zh) * | 2009-09-14 | 2015-08-19 | 皇家飞利浦电子股份有限公司 | 使用大颗粒标记的高灵敏性免疫测定 |
CN101819205A (zh) * | 2010-06-03 | 2010-09-01 | 中国人民解放军第三军医大学 | 人n端b型利钠肽原免疫分析试剂盒及其制备方法 |
AU2011285694B2 (en) * | 2010-08-04 | 2014-12-18 | Idexx Laboratories, Inc. | Detection of degradation products of canine NT-proBNP |
AU2012262154B2 (en) | 2011-05-31 | 2016-08-04 | Idexx Laboratories, Inc. | Detection of degradation products of feline NT-proBNP |
CN102692512A (zh) * | 2012-06-26 | 2012-09-26 | 南京基蛋生物科技有限公司 | NT-proBNP双抗夹心快速检测试剂盒 |
CN109678958B (zh) * | 2019-01-31 | 2022-03-18 | 重庆探生科技有限公司 | 一种人NT-proBNP特异性重组羊单克隆抗体及其制备方法和应用 |
JP2022544394A (ja) | 2019-08-13 | 2022-10-18 | ゲンティアン アクティーゼルスカブ | Nt-プロbnpの定量のための高感度粒子増感アッセイ |
IL311792A (en) | 2021-10-01 | 2024-05-01 | Gentian As | A new method for determining the concentration of N-terminal prohormone BNP (NT-PROBNP) in a sample |
Family Cites Families (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4496654A (en) * | 1983-04-08 | 1985-01-29 | Quidel | Detection of HCG with solid phase support having avidin coating |
US4737453A (en) * | 1984-12-12 | 1988-04-12 | Immunomedics, Inc. | Sandwich immunoassay utilizing a separation specific binding substance |
DE3509958A1 (de) * | 1985-03-20 | 1986-09-25 | Bayer Ag, 5090 Leverkusen | Monoklonale antikoerper gegen atriale, natriuretische peptide vom menschen |
CA1339210C (en) * | 1988-05-31 | 1997-08-05 | John Lewicki | Recombinant techniques for production of novel natriuretic and vasodilator peptides |
GB9211686D0 (en) * | 1992-06-03 | 1992-07-15 | Medisinsk Innovation A S | Chemical compounds |
US6117644A (en) * | 1998-06-04 | 2000-09-12 | Ottawa Heart Institute Research Corporation | Predicting and detecting cardiac allograft rejection |
EP2108177B1 (en) * | 2007-01-26 | 2019-04-10 | Telefonaktiebolaget LM Ericsson (publ) | Border region processing in images |
-
2000
- 2000-01-27 CN CN2007101051759A patent/CN101046478B/zh not_active Expired - Lifetime
- 2000-01-27 DK DK00903642T patent/DK1151304T3/da active
- 2000-01-27 ES ES06010440T patent/ES2312062T3/es not_active Expired - Lifetime
- 2000-01-27 WO PCT/EP2000/000602 patent/WO2000045176A2/de active IP Right Grant
- 2000-01-27 EP EP06010440A patent/EP1698901B1/de not_active Expired - Lifetime
- 2000-01-27 EP EP00903642A patent/EP1151304B9/de not_active Expired - Lifetime
- 2000-01-27 CN CNB008032343A patent/CN1327228C/zh not_active Expired - Lifetime
- 2000-01-27 AT AT00903642T patent/ATE373826T1/de active
- 2000-01-27 CA CA002359667A patent/CA2359667C/en not_active Expired - Lifetime
- 2000-01-27 RU RU2001123936/14A patent/RU2218568C2/ru not_active IP Right Cessation
- 2000-01-27 AT AT06010440T patent/ATE403158T1/de active
- 2000-01-27 DE DE50014666T patent/DE50014666D1/de not_active Expired - Lifetime
- 2000-01-27 AU AU25451/00A patent/AU758562B2/en not_active Expired
- 2000-01-27 HU HU0105195A patent/HU228625B1/hu unknown
- 2000-01-27 IL IL14406200A patent/IL144062A0/xx active IP Right Grant
- 2000-01-27 PL PL364798A patent/PL204235B1/pl unknown
- 2000-01-27 DE DE50015291T patent/DE50015291D1/de not_active Expired - Lifetime
- 2000-01-27 DK DK06010440T patent/DK1698901T3/da active
- 2000-01-27 PT PT06010440T patent/PT1698901E/pt unknown
- 2000-01-27 KR KR1020017009587A patent/KR100572542B1/ko active IP Right Grant
- 2000-01-27 NZ NZ512762A patent/NZ512762A/xx not_active IP Right Cessation
- 2000-01-27 JP JP2000596377A patent/JP3987284B2/ja not_active Expired - Lifetime
- 2000-01-27 ES ES00903642T patent/ES2292426T3/es not_active Expired - Lifetime
-
2001
- 2001-06-28 IL IL144062A patent/IL144062A/en not_active IP Right Cessation
- 2001-07-27 NO NO20013698A patent/NO329866B1/no not_active IP Right Cessation
- 2001-07-27 ZA ZA200106193A patent/ZA200106193B/en unknown
-
2006
- 2006-08-07 US US11/500,555 patent/US20070059767A1/en not_active Abandoned
-
2008
- 2008-10-24 CY CY20081101202T patent/CY1108450T1/el unknown
Also Published As
Similar Documents
Publication | Publication Date | Title |
---|---|---|
NO329866B1 (no) | Fremgangsmate for pavisning av nativt N-terminalt proBNP i en prove som utfores i "sandwich"-format ved anvendelse av minst to antistoffer som gjenkjenner forskjellige epitoper i det native N-terminale proBNP, og som samtidig kan bindes til nativt N-terminalt proBNP, anvendelse av fremgangsmaten for differensiering mellom prover, anvendelse av rekombinant N-terminalt proBNP som standard i en fremgangsmate, antistoffer mot N-terminalt proBNP fremstilt ved immunisering av en egnet organisme med rekombinant fremstilt N-terminalt proBNP, samt cellelinje. | |
US7264938B2 (en) | Method of detecting native proBNP | |
EP1557431B1 (en) | Assay and reagents for quantifying hBNP | |
MXPA01007637A (en) | METHOD OF IDENTIFYING N-TERMINAL proBNP |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MM1K | Lapsed by not paying the annual fees |