CH672796A5 - - Google Patents
Download PDFInfo
- Publication number
- CH672796A5 CH672796A5 CH6700/83A CH670083A CH672796A5 CH 672796 A5 CH672796 A5 CH 672796A5 CH 6700/83 A CH6700/83 A CH 6700/83A CH 670083 A CH670083 A CH 670083A CH 672796 A5 CH672796 A5 CH 672796A5
- Authority
- CH
- Switzerland
- Prior art keywords
- hybrid
- monoclonal antibody
- hybridoma
- antibody
- polydome
- Prior art date
Links
- 210000004408 hybridoma Anatomy 0.000 claims description 114
- 239000000427 antigen Substances 0.000 claims description 97
- 102000036639 antigens Human genes 0.000 claims description 97
- 108091007433 antigens Proteins 0.000 claims description 97
- 210000004027 cell Anatomy 0.000 claims description 83
- 238000000034 method Methods 0.000 claims description 83
- 102000004190 Enzymes Human genes 0.000 claims description 46
- 108090000790 Enzymes Proteins 0.000 claims description 46
- 230000009977 dual effect Effects 0.000 claims description 38
- 230000004927 fusion Effects 0.000 claims description 29
- LPMXVESGRSUGHW-UHFFFAOYSA-N Acolongiflorosid K Natural products OC1C(O)C(O)C(C)OC1OC1CC2(O)CCC3C4(O)CCC(C=5COC(=O)C=5)C4(C)CC(O)C3C2(CO)C(O)C1 LPMXVESGRSUGHW-UHFFFAOYSA-N 0.000 claims description 28
- LPMXVESGRSUGHW-GHYGWZAOSA-N Ouabain Natural products O([C@@H]1[C@@H](O)[C@@H](O)[C@@H](O)[C@H](C)O1)[C@H]1C[C@@H](O)[C@@]2(CO)[C@@](O)(C1)CC[C@H]1[C@]3(O)[C@@](C)([C@H](C4=CC(=O)OC4)CC3)C[C@@H](O)[C@H]21 LPMXVESGRSUGHW-GHYGWZAOSA-N 0.000 claims description 28
- 244000166550 Strophanthus gratus Species 0.000 claims description 28
- LPMXVESGRSUGHW-HBYQJFLCSA-N ouabain Chemical compound O[C@@H]1[C@H](O)[C@@H](O)[C@H](C)O[C@H]1O[C@@H]1C[C@@]2(O)CC[C@H]3[C@@]4(O)CC[C@H](C=5COC(=O)C=5)[C@@]4(C)C[C@@H](O)[C@@H]3[C@@]2(CO)[C@H](O)C1 LPMXVESGRSUGHW-HBYQJFLCSA-N 0.000 claims description 28
- 229960003343 ouabain Drugs 0.000 claims description 28
- 210000001519 tissue Anatomy 0.000 claims description 19
- WYWHKKSPHMUBEB-UHFFFAOYSA-N tioguanine Chemical compound N1C(N)=NC(=S)C2=C1N=CN2 WYWHKKSPHMUBEB-UHFFFAOYSA-N 0.000 claims description 18
- 210000003719 b-lymphocyte Anatomy 0.000 claims description 17
- 238000004519 manufacturing process Methods 0.000 claims description 17
- 239000000126 substance Substances 0.000 claims description 17
- 239000003795 chemical substances by application Substances 0.000 claims description 16
- 239000003112 inhibitor Substances 0.000 claims description 15
- 230000000890 antigenic effect Effects 0.000 claims description 14
- 230000005764 inhibitory process Effects 0.000 claims description 13
- 231100000518 lethal Toxicity 0.000 claims description 10
- 230000001665 lethal effect Effects 0.000 claims description 10
- LPXQRXLUHJKZIE-UHFFFAOYSA-N 8-azaguanine Chemical compound NC1=NC(O)=C2NN=NC2=N1 LPXQRXLUHJKZIE-UHFFFAOYSA-N 0.000 claims description 9
- 229960005508 8-azaguanine Drugs 0.000 claims description 9
- 239000000203 mixture Substances 0.000 claims description 9
- 230000005855 radiation Effects 0.000 claims description 9
- 229960003087 tioguanine Drugs 0.000 claims description 9
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 claims description 8
- 230000002427 irreversible effect Effects 0.000 claims description 8
- 230000035945 sensitivity Effects 0.000 claims description 8
- 206010028980 Neoplasm Diseases 0.000 claims description 7
- 230000002068 genetic effect Effects 0.000 claims description 7
- 239000002738 chelating agent Substances 0.000 claims description 6
- 238000003745 diagnosis Methods 0.000 claims description 6
- 241000894007 species Species 0.000 claims description 6
- 210000004989 spleen cell Anatomy 0.000 claims description 6
- 238000012258 culturing Methods 0.000 claims description 5
- 230000002503 metabolic effect Effects 0.000 claims description 5
- 239000003053 toxin Substances 0.000 claims description 5
- 231100000765 toxin Toxicity 0.000 claims description 5
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 claims description 4
- XEQLGWAGMYUVTR-UHFFFAOYSA-N O=C1NC=NC2=C1NC=N2.C1=CN=C2C(=O)NC(NN)=NC2=N1 Chemical compound O=C1NC=NC2=C1NC=N2.C1=CN=C2C(=O)NC(NN)=NC2=N1 XEQLGWAGMYUVTR-UHFFFAOYSA-N 0.000 claims description 4
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 claims description 4
- 229940104230 thymidine Drugs 0.000 claims description 4
- AGNGYMCLFWQVGX-AGFFZDDWSA-N (e)-1-[(2s)-2-amino-2-carboxyethoxy]-2-diazonioethenolate Chemical group OC(=O)[C@@H](N)CO\C([O-])=C\[N+]#N AGNGYMCLFWQVGX-AGFFZDDWSA-N 0.000 claims description 3
- MWBWWFOAEOYUST-UHFFFAOYSA-N 2-aminopurine Chemical compound NC1=NC=C2N=CNC2=N1 MWBWWFOAEOYUST-UHFFFAOYSA-N 0.000 claims description 3
- 229950011321 azaserine Drugs 0.000 claims description 3
- 108010039491 Ricin Proteins 0.000 claims description 2
- 150000005018 aminopurines Chemical class 0.000 claims 1
- 239000000480 calcium channel blocker Substances 0.000 claims 1
- 229940088598 enzyme Drugs 0.000 description 40
- 239000002609 medium Substances 0.000 description 35
- 238000012360 testing method Methods 0.000 description 24
- 239000000523 sample Substances 0.000 description 21
- 206010003445 Ascites Diseases 0.000 description 17
- 239000011324 bead Substances 0.000 description 15
- 238000006243 chemical reaction Methods 0.000 description 12
- 229940097325 prolactin Drugs 0.000 description 12
- 239000000758 substrate Substances 0.000 description 12
- 102000003946 Prolactin Human genes 0.000 description 11
- 108010057464 Prolactin Proteins 0.000 description 11
- 230000027455 binding Effects 0.000 description 11
- 210000002966 serum Anatomy 0.000 description 11
- 102000018251 Hypoxanthine Phosphoribosyltransferase Human genes 0.000 description 10
- 108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 10
- 229940079593 drug Drugs 0.000 description 10
- 239000003814 drug Substances 0.000 description 10
- 230000008569 process Effects 0.000 description 9
- 238000011534 incubation Methods 0.000 description 8
- 229930193140 Neomycin Natural products 0.000 description 7
- 206010035226 Plasma cell myeloma Diseases 0.000 description 7
- 230000008859 change Effects 0.000 description 7
- 238000001514 detection method Methods 0.000 description 7
- 238000003018 immunoassay Methods 0.000 description 7
- 201000000050 myeloid neoplasm Diseases 0.000 description 7
- 229960004927 neomycin Drugs 0.000 description 7
- 108090000623 proteins and genes Proteins 0.000 description 7
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 230000001263 anti-prolactin effect Effects 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 238000000338 in vitro Methods 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 239000006228 supernatant Substances 0.000 description 6
- 102000005548 Hexokinase Human genes 0.000 description 5
- 108700040460 Hexokinases Proteins 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 5
- 239000002202 Polyethylene glycol Substances 0.000 description 5
- 102000006601 Thymidine Kinase Human genes 0.000 description 5
- 108020004440 Thymidine kinase Proteins 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 238000004925 denaturation Methods 0.000 description 5
- 230000036425 denaturation Effects 0.000 description 5
- 239000001963 growth medium Substances 0.000 description 5
- UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical class O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 5
- 230000002163 immunogen Effects 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 5
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 5
- 229920001223 polyethylene glycol Polymers 0.000 description 5
- 239000013641 positive control Substances 0.000 description 5
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 4
- 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 4
- 102100031126 6-phosphogluconolactonase Human genes 0.000 description 4
- 108010029731 6-phosphogluconolactonase Proteins 0.000 description 4
- NBSCHQHZLSJFNQ-GASJEMHNSA-N D-Glucose 6-phosphate Chemical compound OC1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H](O)[C@H]1O NBSCHQHZLSJFNQ-GASJEMHNSA-N 0.000 description 4
- VFRROHXSMXFLSN-UHFFFAOYSA-N Glc6P Natural products OP(=O)(O)OCC(O)C(O)C(O)C(O)C=O VFRROHXSMXFLSN-UHFFFAOYSA-N 0.000 description 4
- 108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 description 4
- 230000001588 bifunctional effect Effects 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 description 3
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 3
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 3
- DJHGAFSJWGLOIV-UHFFFAOYSA-N Arsenic acid Chemical compound O[As](O)(O)=O DJHGAFSJWGLOIV-UHFFFAOYSA-N 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 229910019142 PO4 Inorganic materials 0.000 description 3
- CXOFVDLJLONNDW-UHFFFAOYSA-N Phenytoin Chemical compound N1C(=O)NC(=O)C1(C=1C=CC=CC=1)C1=CC=CC=C1 CXOFVDLJLONNDW-UHFFFAOYSA-N 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 3
- 229940000488 arsenic acid Drugs 0.000 description 3
- 229940064790 dilantin Drugs 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 238000006911 enzymatic reaction Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000000760 immunoelectrophoresis Methods 0.000 description 3
- 238000009169 immunotherapy Methods 0.000 description 3
- 239000010452 phosphate Substances 0.000 description 3
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 239000007790 solid phase Substances 0.000 description 3
- 210000000130 stem cell Anatomy 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- XTWYTFMLZFPYCI-KQYNXXCUSA-N 5'-adenylphosphoric acid Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O XTWYTFMLZFPYCI-KQYNXXCUSA-N 0.000 description 2
- 102000013563 Acid Phosphatase Human genes 0.000 description 2
- 108010051457 Acid Phosphatase Proteins 0.000 description 2
- 229930024421 Adenine Natural products 0.000 description 2
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 2
- XTWYTFMLZFPYCI-UHFFFAOYSA-N Adenosine diphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(O)=O)C(O)C1O XTWYTFMLZFPYCI-UHFFFAOYSA-N 0.000 description 2
- DJHGAFSJWGLOIV-UHFFFAOYSA-K Arsenate3- Chemical compound [O-][As]([O-])([O-])=O DJHGAFSJWGLOIV-UHFFFAOYSA-K 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 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 2
- 102000008857 Ferritin Human genes 0.000 description 2
- 108050000784 Ferritin Proteins 0.000 description 2
- 238000008416 Ferritin Methods 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 229960000643 adenine Drugs 0.000 description 2
- 229940000489 arsenate Drugs 0.000 description 2
- 230000007910 cell fusion Effects 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000009871 nonspecific binding Effects 0.000 description 2
- 239000012071 phase Substances 0.000 description 2
- 229920002223 polystyrene Polymers 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 238000010791 quenching Methods 0.000 description 2
- 230000000171 quenching effect Effects 0.000 description 2
- 239000000700 radioactive tracer Substances 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 2
- 238000010187 selection method Methods 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- JWDFQMWEFLOOED-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-(pyridin-2-yldisulfanyl)propanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCSSC1=CC=CC=N1 JWDFQMWEFLOOED-UHFFFAOYSA-N 0.000 description 1
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 1
- STQGQHZAVUOBTE-UHFFFAOYSA-N 7-Cyan-hept-2t-en-4,6-diinsaeure Natural products C1=2C(O)=C3C(=O)C=4C(OC)=CC=CC=4C(=O)C3=C(O)C=2CC(O)(C(C)=O)CC1OC1CC(N)C(O)C(C)O1 STQGQHZAVUOBTE-UHFFFAOYSA-N 0.000 description 1
- ZKHQWZAMYRWXGA-KQYNXXCUSA-J ATP(4-) Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-J 0.000 description 1
- 108091006112 ATPases Proteins 0.000 description 1
- 102000057290 Adenosine Triphosphatases Human genes 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- WEAHRLBPCANXCN-UHFFFAOYSA-N Daunomycin Natural products CCC1(O)CC(OC2CC(N)C(O)C(C)O2)c3cc4C(=O)c5c(OC)cccc5C(=O)c4c(O)c3C1 WEAHRLBPCANXCN-UHFFFAOYSA-N 0.000 description 1
- 238000009007 Diagnostic Kit Methods 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 108700004714 Gelonium multiflorum GEL Proteins 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 206010019695 Hepatic neoplasm Diseases 0.000 description 1
- 108010001336 Horseradish Peroxidase 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
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 241000283977 Oryctolagus Species 0.000 description 1
- 108030004873 Phosphoribosylformylglycinamidine synthases Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 101710119110 Prolactin-1 Proteins 0.000 description 1
- 238000010266 Sephadex chromatography Methods 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 102100037409 Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1 Human genes 0.000 description 1
- 101710116672 Sushi, von Willebrand factor type A, EGF and pentraxin domain-containing protein 1 Proteins 0.000 description 1
- 101150003725 TK gene Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 210000003567 ascitic fluid Anatomy 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 238000012832 cell culture technique Methods 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000005515 coenzyme Substances 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- 239000013068 control sample Substances 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- STQGQHZAVUOBTE-VGBVRHCVSA-N daunorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(C)=O)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 STQGQHZAVUOBTE-VGBVRHCVSA-N 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 235000019800 disodium phosphate Nutrition 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000007499 fusion processing Methods 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- PPTXFSQSISUDAU-UHFFFAOYSA-M hydrogen sulfate;2-methyl-4-[(2-methylphenyl)diazenyl]benzenediazonium Chemical compound OS([O-])(=O)=O.CC1=CC=CC=C1N=NC1=CC=C([N+]#N)C(C)=C1 PPTXFSQSISUDAU-UHFFFAOYSA-M 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000013198 immunometric assay Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 231100000636 lethal dose Toxicity 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 208000014018 liver neoplasm Diseases 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 238000004020 luminiscence type Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 239000011824 nuclear material Substances 0.000 description 1
- 238000011580 nude mouse model Methods 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- WFLQAMUOBIONDG-UHFFFAOYSA-N phenoxyarsonic acid Chemical compound O[As](O)(=O)OC1=CC=CC=C1 WFLQAMUOBIONDG-UHFFFAOYSA-N 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- WGJJROVFWIXTPA-OALUTQOASA-N prostanoic acid Chemical compound CCCCCCCC[C@H]1CCC[C@@H]1CCCCCCC(O)=O WGJJROVFWIXTPA-OALUTQOASA-N 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 238000004153 renaturation Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical class CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
- C07K16/468—Immunoglobulins having two or more different antigen binding sites, e.g. multifunctional antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K51/00—Preparations containing radioactive substances for use in therapy or testing in vivo
- A61K51/02—Preparations containing radioactive substances for use in therapy or testing in vivo characterised by the carrier, i.e. characterised by the agent or material covalently linked or complexing the radioactive nucleus
- A61K51/04—Organic compounds
- A61K51/08—Peptides, e.g. proteins, carriers being peptides, polyamino acids, proteins
- A61K51/10—Antibodies or immunoglobulins; Fragments thereof, the carrier being an antibody, an immunoglobulin or a fragment thereof, e.g. a camelised human single domain antibody or the Fc fragment of an antibody
- A61K51/1084—Antibodies or immunoglobulins; Fragments thereof, the carrier being an antibody, an immunoglobulin or a fragment thereof, e.g. a camelised human single domain antibody or the Fc fragment of an antibody the antibody being a hybrid immunoglobulin
- A61K51/109—Antibodies or immunoglobulins; Fragments thereof, the carrier being an antibody, an immunoglobulin or a fragment thereof, e.g. a camelised human single domain antibody or the Fc fragment of an antibody the antibody being a hybrid immunoglobulin immunoglobulins having two or more different antigen-binding sites or multifunctional antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K2123/00—Preparations for testing in vivo
Landscapes
- Health & Medical Sciences (AREA)
- Immunology (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Epidemiology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Physics & Mathematics (AREA)
- Optics & Photonics (AREA)
- Pharmacology & Pharmacy (AREA)
- Molecular Biology (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US36778482A | 1982-04-12 | 1982-04-12 |
Publications (1)
Publication Number | Publication Date |
---|---|
CH672796A5 true CH672796A5 (it) | 1989-12-29 |
Family
ID=23448582
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CH6700/83A CH672796A5 (it) | 1982-04-12 | 1983-04-12 |
Country Status (11)
Country | Link |
---|---|
EP (1) | EP0105360A4 (it) |
JP (2) | JPH0753119B2 (it) |
AT (1) | AT394577B (it) |
AU (1) | AU550486B2 (it) |
CA (1) | CA1213229A (it) |
CH (1) | CH672796A5 (it) |
ES (7) | ES521370A0 (it) |
FI (1) | FI834529A0 (it) |
GB (4) | GB2128631B (it) |
IT (1) | IT1219778B (it) |
WO (1) | WO1983003679A1 (it) |
Families Citing this family (61)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP3177776B2 (ja) * | 1988-09-27 | 2001-06-18 | 武田薬品工業株式会社 | ハイブリッドモノクローナル抗体,抗体産生ポリドーマおよび抗体含有薬剤 |
US5292668A (en) * | 1981-12-21 | 1994-03-08 | Boston Biomedical Research Institute, Inc. | Bispecific antibody determinants |
IL70686A (en) * | 1983-01-20 | 1988-07-31 | Suntory Ltd | Mutant tumor cell lines for use in the preparation of hybridomas and the hybridomas obtained therefrom |
GB2148299B (en) * | 1983-09-01 | 1988-01-06 | Hybritech Inc | Antibody compositions of therapeutic agents having an extended serum half-life |
EP0467416A1 (en) * | 1983-09-01 | 1992-01-22 | Hybritech Incorporated | Antibody compositions of therapeutic agents having an extended serum half-life |
AU595159B2 (en) * | 1984-04-23 | 1990-03-29 | Boston Biomedical Research Institute Incorporated | Bispecific antibody determinants |
NL8501219A (nl) * | 1985-04-29 | 1986-11-17 | Stichting Vrienden Van De Stic | Immunologisch complex, de bereiding en toepassing daarvan. |
EP0241907A3 (en) | 1986-04-14 | 1989-09-13 | The General Hospital Corporation | Heterobifunctional antibodies and method of use |
US5453269A (en) * | 1986-04-14 | 1995-09-26 | The General Hospital Corporation | Heterobifunctional antibodies having dual specificity for fibrin and thrombolylic agents and methods of use |
FR2604092B1 (fr) * | 1986-09-19 | 1990-04-13 | Immunotech Sa | Immunoreactifs destines a cibler les cellules animales pour leur visualisation ou leur destruction in vivo |
GB8626413D0 (en) * | 1986-11-05 | 1986-12-03 | Gilliland L K | Antibodies |
GB8626412D0 (en) * | 1986-11-05 | 1986-12-03 | Clark M R | Antibodies |
US5053226A (en) * | 1987-07-15 | 1991-10-01 | Board Of Regents, The University Of Texas System | Monoclonal antibodies binding platinum complexes |
JP2755395B2 (ja) * | 1987-09-23 | 1998-05-20 | ブリストル―マイアーズ スクイブ コムパニー | Hiv感染細胞に殺作用する抗体異種結合体 |
GB2218100A (en) * | 1988-03-02 | 1989-11-08 | Erling Sundrehagen | Conjugates for the detection and/or quantification of antigenic substances in body fluids |
US4892824A (en) * | 1988-03-15 | 1990-01-09 | Synbiotics Corporation | Fast track method for producing monoclonal bi-specific immunoglobulins |
US5582862A (en) * | 1988-04-04 | 1996-12-10 | General Hospital Corporation | Antibodies that bind to α2-antiplasmin crosslinked to fibrin which do not inhibit plasma α2-antiplasmin |
US5372812A (en) * | 1988-04-04 | 1994-12-13 | The General Hospital Corporation | Composition and method for acceleration of clot lysis |
JPH02196799A (ja) * | 1988-04-08 | 1990-08-03 | Agency Of Ind Science & Technol | 抗ヒト癌蛋白複合体 |
US5851527A (en) * | 1988-04-18 | 1998-12-22 | Immunomedics, Inc. | Method for antibody targeting of therapeutic agents |
IT1235349B (it) * | 1988-12-23 | 1992-06-30 | Biodata Spa | Saggio immunologico per determinazioni in fase omogenea |
US5217713A (en) * | 1988-12-27 | 1993-06-08 | Takeda Chemical Industries, Ltd. | Cytotoxic bispecific monoclonal antibody, its production and use |
CA2006408A1 (en) * | 1988-12-27 | 1990-06-27 | Susumu Iwasa | Bispecific monoclonal antibody, its production and use |
WO1990012109A1 (en) * | 1989-03-30 | 1990-10-18 | Board Of Regents, The University Of Texas System | Monoclonal antibodies binding platinum complexes |
FR2652004B1 (fr) * | 1989-09-21 | 1994-10-28 | Immunotech Partners | Nouveaux derives hydrophiles, application au diagnostic et a la therapeutique, kits diagnostiques ou therapeutiques et reactifs immunologiques. |
DE69130561T2 (de) * | 1990-02-16 | 1999-06-24 | Boston Biomedical Research Institute, Inc., Boston, Mass. | Hybride Reagenzien mit der Fähigkeit, Moleküle selektiv in Zellen freizusetzen |
TW212184B (it) * | 1990-04-02 | 1993-09-01 | Takeda Pharm Industry Co Ltd | |
US5573920A (en) * | 1991-04-26 | 1996-11-12 | Surface Active Limited | Antibodies, and methods for their use |
GB9316369D0 (en) * | 1993-08-06 | 1993-09-22 | Surface Active Ltd | Diagnostic method |
US5541110A (en) | 1994-05-17 | 1996-07-30 | Bristol-Myers Squibb | Cloning and expression of a gene encoding bryodin 1 from Bryonia dioica |
GB9421468D0 (en) * | 1994-10-18 | 1994-12-07 | Surface Active Ltd | Biosensor |
EP0937146A2 (en) * | 1996-09-20 | 1999-08-25 | The General Hospital Corporation | Composition and method for enhancing fibrinolysis using antibodies to alpha-2-antiplasmin |
US20020132274A1 (en) | 2001-01-17 | 2002-09-19 | Nevalainen Marja T. | Diagnostic and monitorings methods for cancer |
US7659241B2 (en) | 2002-07-31 | 2010-02-09 | Seattle Genetics, Inc. | Drug conjugates and their use for treating cancer, an autoimmune disease or an infectious disease |
US7498298B2 (en) | 2003-11-06 | 2009-03-03 | Seattle Genetics, Inc. | Monomethylvaline compounds capable of conjugation to ligands |
US7932242B2 (en) | 2004-03-16 | 2011-04-26 | Temple University - Of The Commonwealth System Of Higher Education | Substituted phenoxy-and phenylthio-derivatives for treating proliferative disorders |
JP2008519863A (ja) | 2004-11-12 | 2008-06-12 | シアトル ジェネティクス インコーポレイティッド | N末端にアミノ安息香酸単位を有するオーリスタチン |
EP2511299A1 (en) | 2005-04-19 | 2012-10-17 | Seattle Genetics, Inc. | Humanized anti-CD70 binding agents and uses thereof |
EP4026840A1 (en) | 2005-07-18 | 2022-07-13 | Seagen Inc. | Beta-glucuronide-linker drug conjugates |
EP2609932B1 (en) | 2006-12-01 | 2022-02-02 | Seagen Inc. | Variant target binding agents and uses thereof |
ZA200904482B (en) | 2007-01-22 | 2010-09-29 | Genentech Inc | Polyelectrolyte precipitation and purification of antibodies |
AU2009242453B2 (en) | 2008-05-02 | 2014-12-04 | Seagen Inc. | Methods and compositions for making antibodies and antibody derivatives with reduced core fucosylation |
WO2011133658A1 (en) | 2010-04-22 | 2011-10-27 | Boston Medical Center Corporation | Compositions and methods for targeting and delivering therapeutics into cells |
WO2014089177A2 (en) | 2012-12-04 | 2014-06-12 | Massachusetts Institute Of Technology | Compounds, conjugates and compositions of epipolythiodiketopiperazines and polythiodiketopiperazines |
MY174813A (en) | 2013-03-15 | 2020-05-16 | Zymeworks Inc | Cytotoxic and anti-mitotic compounds, and methods of using the same |
JP6473418B2 (ja) | 2013-10-10 | 2019-02-20 | 幸成 加藤 | 抗ポドプラニン抗体 |
CN106255513B (zh) | 2013-12-27 | 2022-01-14 | 酵活有限公司 | 用于药物偶联物的含磺酰胺连接*** |
AU2015318556C1 (en) | 2014-09-17 | 2021-01-07 | Zymeworks Bc Inc. | Cytotoxic and anti-mitotic compounds, and methods of using the same |
US10618935B2 (en) | 2015-11-03 | 2020-04-14 | Industrial Technology Research Institute | Antibody-drug conjugate (ADC) and method for forming the same |
SG11201807827VA (en) | 2016-03-25 | 2018-10-30 | Seattle Genetics Inc | Process for the preparation of pegylated drug-linkers and intermediates thereof |
US10918627B2 (en) | 2016-05-11 | 2021-02-16 | Massachusetts Institute Of Technology | Convergent and enantioselective total synthesis of Communesin analogs |
MX2019010769A (es) | 2017-03-24 | 2019-12-11 | Seattle Genetics Inc | Proceso para la preparacion de enlazadores de farmacos de glucuronidos y compuestos intermediarios de los mismos. |
US11932650B2 (en) | 2017-05-11 | 2024-03-19 | Massachusetts Institute Of Technology | Potent agelastatin derivatives as modulators for cancer invasion and metastasis |
US10640508B2 (en) | 2017-10-13 | 2020-05-05 | Massachusetts Institute Of Technology | Diazene directed modular synthesis of compounds with quaternary carbon centers |
CA3110096A1 (en) | 2018-08-30 | 2020-03-05 | Innovative Cellular Therapeutics CO., LTD. | Chimeric antigen receptor cells for treating solid tumor |
US20220409734A1 (en) | 2019-05-10 | 2022-12-29 | Yutaka Nishimoto | Antibody drug conjugates |
TW202138388A (zh) | 2019-12-30 | 2021-10-16 | 美商西根公司 | 以非海藻糖苷化抗-cd70抗體治療癌症之方法 |
US12043654B2 (en) | 2020-06-02 | 2024-07-23 | Innovative Cellular Therapeutics Holdings, Ltd. | Anti-GCC antibody and CAR thereof for treating digestive system cancer |
WO2022097117A1 (en) | 2020-11-09 | 2022-05-12 | Takeda Pharmaceutical Company Ltd. | Antibody drug conjugates |
WO2022182415A1 (en) | 2021-02-24 | 2022-09-01 | Massachusetts Institute Of Technology | Himastatin derivatives, and processes of preparation thereof, and uses thereof |
WO2023278377A1 (en) | 2021-06-29 | 2023-01-05 | Seagen Inc. | Methods of treating cancer with a combination of a nonfucosylated anti-cd70 antibody and a cd47 antagonist |
Family Cites Families (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4130634A (en) * | 1974-03-15 | 1978-12-19 | University Of Illinois Foundation | Method for detecting and quantifying antigens |
US4331647A (en) * | 1980-03-03 | 1982-05-25 | Goldenberg Milton David | Tumor localization and therapy with labeled antibody fragments specific to tumor-associated markers |
US4376110A (en) * | 1980-08-04 | 1983-03-08 | Hybritech, Incorporated | Immunometric assays using monoclonal antibodies |
US4474893A (en) * | 1981-07-01 | 1984-10-02 | The University of Texas System Cancer Center | Recombinant monoclonal antibodies |
-
1983
- 1983-04-11 ES ES521370A patent/ES521370A0/es active Granted
- 1983-04-11 CA CA000425558A patent/CA1213229A/en not_active Expired
- 1983-04-12 WO PCT/US1983/000525 patent/WO1983003679A1/en not_active Application Discontinuation
- 1983-04-12 GB GB08332646A patent/GB2128631B/en not_active Expired
- 1983-04-12 EP EP19830901672 patent/EP0105360A4/en not_active Ceased
- 1983-04-12 IT IT20548/83A patent/IT1219778B/it active
- 1983-04-12 AU AU15559/83A patent/AU550486B2/en not_active Expired
- 1983-04-12 CH CH6700/83A patent/CH672796A5/de not_active IP Right Cessation
- 1983-04-12 AT AT0901883A patent/AT394577B/de not_active IP Right Cessation
- 1983-12-09 FI FI834529A patent/FI834529A0/fi not_active Application Discontinuation
- 1983-12-12 ES ES527963A patent/ES8503441A1/es not_active Expired
-
1984
- 1984-07-02 ES ES533930A patent/ES8603080A1/es not_active Expired
- 1984-07-02 ES ES533931A patent/ES533931A0/es active Granted
- 1984-10-31 ES ES537257A patent/ES8606655A1/es not_active Expired
- 1984-12-18 ES ES538727A patent/ES8604424A1/es not_active Expired
-
1985
- 1985-07-16 ES ES545247A patent/ES8607386A1/es not_active Expired
- 1985-12-09 GB GB08530310A patent/GB2167086B/en not_active Expired
- 1985-12-09 GB GB08530308A patent/GB2168998B/en not_active Expired
- 1985-12-09 GB GB08530309A patent/GB2169921B/en not_active Expired
-
1987
- 1987-01-05 JP JP62000342A patent/JPH0753119B2/ja not_active Expired - Lifetime
-
1994
- 1994-02-10 JP JP6016728A patent/JP2562002B2/ja not_active Expired - Lifetime
Also Published As
Similar Documents
Publication | Publication Date | Title |
---|---|---|
AT394577B (de) | Polydom, verfahren zu seiner herstellung und immunodiagnostische verfahren | |
DE3751432T2 (de) | Rezeptoren für Immunkomplexe, Verfahren zur ihrer Herstellung und Verfahren zur Prüfung diese benutzend. | |
DE69214709T2 (de) | Neue Antikörper und Verfahren zu ihrer Verwendung | |
DE3854194T2 (de) | Monoklonale antikörper gegen glykosyliertes albumin, hybride zellinien, die diese antikörper produzieren, sowie deren verwendung. | |
DE3783928T2 (de) | Verfahren zur immunoassay. | |
DE69824178T2 (de) | Verfahren zur specifischen bestimmung der c-peptide | |
DE3750389T2 (de) | Antikörper gegen menschlichen progesteronrezeptor sowie diagnosematerial und -verfahren. | |
EP0134552B1 (de) | Monoklonaler Antikörper mit hoher Affinität zum Digoxin | |
DE3205849C2 (de) | Reagens zur immunologischen Bestimmung | |
JPS60228962A (ja) | 複数の抗体を同時に検出する為の方法 | |
EP0449269B1 (de) | Verfahren zum Nachweis von phosphoryliertes Tyrosin enthaltenden Proteinen | |
DE69427122T2 (de) | Kompetitiver immunotest unter verwendung eines bindenden proteins in multiklonaler antikoerperstruktur | |
EP0547059B1 (de) | Pankreas-elastase-1-spezifischer antikörper, ein verfahren zu seiner gewinnung und ein testkit der solche antikörper enthält | |
DE69008178T2 (de) | Analyse von vitamin b12. | |
DE4008546C2 (it) | ||
DE60036452T2 (de) | Monoklonaler anti-uracil antikörper | |
DE69110067T2 (de) | Monoklonale Antikörper gegen nicht-A 1C glykosyliertes Hämoglobin. | |
DE60318271T2 (de) | Antikörper gegen allgegenwärtige mitochondriale Kreatinkinase und dessen Verwendung | |
DE3820556A1 (de) | Verfahren zur bestimmung von allergenspezifischen antikoerpern in koerperfluessigkeiten | |
DE3686068T2 (de) | Verfahren zur bestimmung von menschlicher prolyl-4-hydroxylase durch immunotest. | |
DE3036184A1 (de) | Reagenz und verfahren zur bestimmung von human-muskeltyp-aldolase | |
EP0182888B1 (de) | Verfahren und reagenz zur differenzierten bestimmung von isoenzymen der alkalischen phosphatase sowie hierzu geeigneter monoklonaler antikörper | |
JPS59500696A (ja) | 二重特異性を有する抗体、その製造及びその用途 | |
DE4119395C2 (de) | Monoklonaler Antikörper, der gegen delta-Bilirubin spezifisch ist, seine Verwendung zur Bestimmung von delta-Bilirubin und die entsprechende Antikörperproduzierende Hybridomazellinie | |
DE68909276T2 (de) | Monoklonale Antikörper, geeignet für den aus der menschlichen Bauchspeicheldrüse sekretierten Trypsin-Inhibitor, Hybridomen, die diese produzieren und ihre Herstellung und Verwendung. |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
PL | Patent ceased |