NZ221230A - Method for assaying biological material using antibodies to terminal n-acetyl glucosamine groups - Google Patents
Method for assaying biological material using antibodies to terminal n-acetyl glucosamine groupsInfo
- Publication number
- NZ221230A NZ221230A NZ221230A NZ22123087A NZ221230A NZ 221230 A NZ221230 A NZ 221230A NZ 221230 A NZ221230 A NZ 221230A NZ 22123087 A NZ22123087 A NZ 22123087A NZ 221230 A NZ221230 A NZ 221230A
- Authority
- NZ
- New Zealand
- Prior art keywords
- label
- acetyl
- terminal
- biological material
- bound
- Prior art date
Links
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical group CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 title claims abstract description 34
- 239000012620 biological material Substances 0.000 title claims abstract description 24
- 238000000034 method Methods 0.000 title claims description 26
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 31
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 31
- 241001505901 Streptococcus sp. 'group A' Species 0.000 claims abstract description 10
- 210000004027 cell Anatomy 0.000 claims description 18
- 102000004190 Enzymes Human genes 0.000 claims description 14
- 108090000790 Enzymes Proteins 0.000 claims description 14
- 102000004169 proteins and genes Human genes 0.000 claims description 12
- 108090000623 proteins and genes Proteins 0.000 claims description 12
- 239000000463 material Substances 0.000 claims description 7
- 239000007787 solid Substances 0.000 claims description 6
- 108090000288 Glycoproteins Proteins 0.000 claims description 4
- 102000003886 Glycoproteins Human genes 0.000 claims description 4
- 238000006243 chemical reaction Methods 0.000 claims description 3
- 210000004962 mammalian cell Anatomy 0.000 claims description 3
- 239000012528 membrane Substances 0.000 claims description 3
- 101710120037 Toxin CcdB Proteins 0.000 claims description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 claims 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 claims 1
- 229940072221 immunoglobulins Drugs 0.000 abstract description 12
- 210000002421 cell wall Anatomy 0.000 abstract description 9
- 206010039073 rheumatoid arthritis Diseases 0.000 abstract description 9
- 208000011231 Crohn disease Diseases 0.000 abstract description 3
- 238000001514 detection method Methods 0.000 abstract description 2
- 201000010099 disease Diseases 0.000 abstract description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 2
- 238000003745 diagnosis Methods 0.000 abstract 1
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 16
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 description 16
- 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 15
- 239000002953 phosphate buffered saline Substances 0.000 description 15
- 229940088598 enzyme Drugs 0.000 description 12
- 229950006780 n-acetylglucosamine Drugs 0.000 description 12
- 239000000020 Nitrocellulose Substances 0.000 description 11
- 229920001220 nitrocellulos Polymers 0.000 description 11
- 102000013361 fetuin Human genes 0.000 description 10
- 108060002885 fetuin Proteins 0.000 description 10
- 238000003556 assay Methods 0.000 description 9
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 8
- 241000699670 Mus sp. Species 0.000 description 8
- 206010028980 Neoplasm Diseases 0.000 description 7
- 230000002159 abnormal effect Effects 0.000 description 7
- 235000000346 sugar Nutrition 0.000 description 6
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 4
- OVRNDRQMDRJTHS-RTRLPJTCSA-N N-acetyl-D-glucosamine Chemical compound CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-RTRLPJTCSA-N 0.000 description 4
- 102000005348 Neuraminidase Human genes 0.000 description 4
- 108010006232 Neuraminidase Proteins 0.000 description 4
- 229940098773 bovine serum albumin Drugs 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 3
- 241000282346 Meles meles Species 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 102000003992 Peroxidases Human genes 0.000 description 3
- 206010035226 Plasma cell myeloma Diseases 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 201000000050 myeloid neoplasm Diseases 0.000 description 3
- 108040007629 peroxidase activity proteins Proteins 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 229920000136 polysorbate Polymers 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 201000008827 tuberculosis Diseases 0.000 description 3
- GEYOCULIXLDCMW-UHFFFAOYSA-N 1,2-phenylenediamine Chemical compound NC1=CC=CC=C1N GEYOCULIXLDCMW-UHFFFAOYSA-N 0.000 description 2
- LVSPDZAGCBEQAV-UHFFFAOYSA-N 4-chloronaphthalen-1-ol Chemical compound C1=CC=C2C(O)=CC=C(Cl)C2=C1 LVSPDZAGCBEQAV-UHFFFAOYSA-N 0.000 description 2
- 206010006049 Bovine Tuberculosis Diseases 0.000 description 2
- 241001274613 Corvus frugilegus Species 0.000 description 2
- 102000002464 Galactosidases Human genes 0.000 description 2
- 108010093031 Galactosidases Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 238000001641 gel filtration chromatography Methods 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 238000009169 immunotherapy Methods 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 229920002223 polystyrene Polymers 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 210000004989 spleen cell Anatomy 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- YMXHPSHLTSZXKH-RVBZMBCESA-N (2,5-dioxopyrrolidin-1-yl) 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoate Chemical compound C([C@H]1[C@H]2NC(=O)N[C@H]2CS1)CCCC(=O)ON1C(=O)CCC1=O YMXHPSHLTSZXKH-RVBZMBCESA-N 0.000 description 1
- YYGNTYWPHWGJRM-UHFFFAOYSA-N (6E,10E,14E,18E)-2,6,10,15,19,23-hexamethyltetracosa-2,6,10,14,18,22-hexaene Chemical compound CC(C)=CCCC(C)=CCCC(C)=CCCC=C(C)CCC=C(C)CCC=C(C)C YYGNTYWPHWGJRM-UHFFFAOYSA-N 0.000 description 1
- -1 0-galactosidase Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 206010005003 Bladder cancer Diseases 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- 241000220451 Canavalia Species 0.000 description 1
- 235000010520 Canavalia ensiformis Nutrition 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 101710112752 Cytotoxin Proteins 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 1
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 1
- 206010024229 Leprosy Diseases 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- MSFSPUZXLOGKHJ-UHFFFAOYSA-N Muraminsaeure Natural products OC(=O)C(C)OC1C(N)C(O)OC(CO)C1O MSFSPUZXLOGKHJ-UHFFFAOYSA-N 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000187479 Mycobacterium tuberculosis Species 0.000 description 1
- VQWPZBYYHBLMRB-RQICVUQASA-N N[C@@]1(C(O)(O[C@@H]([C@H]([C@@H]1O)O)CO)C1=CC=CC=C1)NC(C)=O Chemical compound N[C@@]1(C(O)(O[C@@H]([C@H]([C@@H]1O)O)CO)C1=CC=CC=C1)NC(C)=O VQWPZBYYHBLMRB-RQICVUQASA-N 0.000 description 1
- 241001524178 Paenarthrobacter ureafaciens Species 0.000 description 1
- 108010013639 Peptidoglycan Proteins 0.000 description 1
- BHEOSNUKNHRBNM-UHFFFAOYSA-N Tetramethylsqualene Natural products CC(=C)C(C)CCC(=C)C(C)CCC(C)=CCCC=C(C)CCC(C)C(=C)CCC(C)C(C)=C BHEOSNUKNHRBNM-UHFFFAOYSA-N 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 1
- 241000306909 Zeala Species 0.000 description 1
- 230000003187 abdominal effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 125000003172 aldehyde group Chemical group 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 239000011545 carbonate/bicarbonate buffer Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000012937 correction Methods 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
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 231100000599 cytotoxic agent Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 239000002619 cytotoxin Substances 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- PRAKJMSDJKAYCZ-UHFFFAOYSA-N dodecahydrosqualene Natural products CC(C)CCCC(C)CCCC(C)CCCCC(C)CCCC(C)CCCC(C)C PRAKJMSDJKAYCZ-UHFFFAOYSA-N 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000001493 electron microscopy Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000002134 immunopathologic effect Effects 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- 210000000066 myeloid cell Anatomy 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000003307 slaughter Methods 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 229940031439 squalene Drugs 0.000 description 1
- TUHBEKDERLKLEC-UHFFFAOYSA-N squalene Natural products CC(=CCCC(=CCCC(=CCCC=C(/C)CCC=C(/C)CC=C(C)C)C)C)C TUHBEKDERLKLEC-UHFFFAOYSA-N 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 201000005112 urinary bladder cancer Diseases 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/564—Immunoassay; Biospecific binding assay; Materials therefor for pre-existing immune complex or autoimmune disease, i.e. systemic lupus erythematosus, rheumatoid arthritis, multiple sclerosis, rheumatoid factors or complement components C1-C9
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1267—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria
- C07K16/1275—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-positive bacteria from Streptococcus (G)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Hematology (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Urology & Nephrology (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Rheumatology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Food Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Rehabilitation Therapy (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB868618443A GB8618443D0 (en) | 1986-07-29 | 1986-07-29 | Monoclonal antibodies |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NZ221230A true NZ221230A (en) | 1990-04-26 |
Family
ID=10601843
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NZ221230A NZ221230A (en) | 1986-07-29 | 1987-07-28 | Method for assaying biological material using antibodies to terminal n-acetyl glucosamine groups |
Country Status (13)
Families Citing this family (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5622871A (en) | 1987-04-27 | 1997-04-22 | Unilever Patent Holdings B.V. | Capillary immunoassay and device therefor comprising mobilizable particulate labelled reagents |
| US5271927A (en) * | 1986-02-13 | 1993-12-21 | Celltech Limited | Antibody conjugates with macrocyclic ligands |
| CA1303983C (en) * | 1987-03-27 | 1992-06-23 | Robert W. Rosenstein | Solid phase assay |
| ATE195022T1 (de) | 1987-04-27 | 2000-08-15 | Unilever Nv | Spezifische bindungstestverfahren |
| US4855240A (en) * | 1987-05-13 | 1989-08-08 | Becton Dickinson And Company | Solid phase assay employing capillary flow |
| GB8719042D0 (en) | 1987-08-12 | 1987-09-16 | Parker D | Conjugate compounds |
| GB8719041D0 (en) * | 1987-08-12 | 1987-09-16 | Parker D | Conjugate compounds |
| GB8726271D0 (en) * | 1987-11-10 | 1987-12-16 | Univ London | Protein glycosylation assay |
| US5342936A (en) * | 1989-02-10 | 1994-08-30 | David Parker | Tetra-aza macrocycles and processes for their preparation |
| US6352862B1 (en) | 1989-02-17 | 2002-03-05 | Unilever Patent Holdings B.V. | Analytical test device for imuno assays and methods of using same |
| US5247077A (en) * | 1989-06-23 | 1993-09-21 | Celltech Limited | Tri-aza macrocycles and processes for their preparation |
| JPH0726963B2 (ja) * | 1989-12-28 | 1995-03-29 | 丸善石油化学株式会社 | 悪性腫瘍に対する抗体、及びこの抗体を用いた悪性腫瘍の判別方法 |
| WO2000061636A2 (en) * | 1999-04-14 | 2000-10-19 | Research Corporation Technologies, Inc. | Aberrantly glycosylated antibodies as marker for cancer |
| GB0002660D0 (en) * | 2000-02-04 | 2000-03-29 | Biomade B V | Method of stabilizing a hydrophobin-containing solution and a method of coatinga surface with a hydrophobin |
| IL154853A0 (en) * | 2000-10-27 | 2003-10-31 | Chiron Spa | Nucleic acids and proteins from streptococcus groups a & b |
| FI20011671A7 (fi) | 2001-08-20 | 2003-02-21 | Carbion Oy | Tuumorispesifiset oligosakkaridisekvenssit ja niiden käyttö |
| EP2322209A3 (en) * | 2002-08-20 | 2012-02-01 | Glykos Finland Oy | Tumor specific oligosaccharide epitopes and use thereof |
| CA3215117A1 (en) | 2021-04-01 | 2022-10-06 | Becton, Dickinson And Company | Methods for enhancing specificity and sensitivity of group a streptococcus immunoassay |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3790447A (en) * | 1972-07-05 | 1974-02-05 | Abbott Lab | Streptococci diagnostic method |
| SE7712244L (sv) * | 1977-10-31 | 1979-05-01 | Jonsson U R S | Forfarande for framstellning av preparationer av avdodade bakterier |
| US4292296A (en) | 1978-09-12 | 1981-09-29 | Baxter Travenol Laboratories, Inc. | Diagnostic method |
| GB2093993A (en) | 1980-07-25 | 1982-09-08 | Otsuka Pharma Co Ltd | Method for determining tumor-associated glucose side chain method for diagnosing tumors and kit for diagnosing tumors |
| US4489167A (en) * | 1981-06-02 | 1984-12-18 | Baxter Travenol Laboratories, Inc. | Methods and compositions for cancer detection |
| EP0114818B1 (en) * | 1982-08-09 | 1987-08-12 | Centocor, Inc. | Immunoassay for carbohydrate antigenic determinant |
| EP0141818A1 (en) * | 1983-04-18 | 1985-05-22 | Quidel | Removal of self-binding and staph a cross-reactivity of anti-strep antibody |
| JPS608228A (ja) * | 1983-06-28 | 1985-01-17 | Kyowa Hakko Kogyo Co Ltd | モノクロ−ナル抗体 |
| CA1231050A (en) * | 1984-01-27 | 1988-01-05 | Joseph W. Holland | PROCEDURE FOR DETECTING .beta.-HEMOLYTIC STREPTOCOCCUS ANTIGENS |
| US4618576A (en) * | 1984-02-27 | 1986-10-21 | Becton Dickinson And Company | Diagnostic test for Streptococcus A |
| US4659659A (en) * | 1985-01-22 | 1987-04-21 | Monsanto Company | Diagnostic method for diseases having an arthritic component |
-
1986
- 1986-07-29 GB GB868618443A patent/GB8618443D0/en active Pending
-
1987
- 1987-07-28 DE DE8787306664T patent/DE3779207D1/de not_active Expired - Fee Related
- 1987-07-28 IE IE204187A patent/IE59984B1/en not_active IP Right Cessation
- 1987-07-28 ZA ZA875551A patent/ZA875551B/xx unknown
- 1987-07-28 AT AT87306664T patent/ATE76512T1/de not_active IP Right Cessation
- 1987-07-28 GB GB8717792A patent/GB2195343B/en not_active Expired - Lifetime
- 1987-07-28 AU AU76267/87A patent/AU601455B2/en not_active Ceased
- 1987-07-28 DK DK392387A patent/DK392387A/da not_active Application Discontinuation
- 1987-07-28 ES ES198787306664T patent/ES2032447T3/es not_active Expired - Lifetime
- 1987-07-28 EP EP87306664A patent/EP0255342B1/en not_active Expired - Lifetime
- 1987-07-28 NZ NZ221230A patent/NZ221230A/en unknown
- 1987-07-29 JP JP62187856A patent/JPS63119498A/ja active Pending
-
1992
- 1992-08-20 GR GR920401195T patent/GR3005450T3/el unknown
-
1993
- 1993-03-10 US US08/031,075 patent/US6391634B1/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JPS63119498A (ja) | 1988-05-24 |
| GB8618443D0 (en) | 1986-09-03 |
| AU601455B2 (en) | 1990-09-13 |
| DK392387D0 (da) | 1987-07-28 |
| GB2195343B (en) | 1990-08-01 |
| GR3005450T3 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1993-05-24 |
| DE3779207D1 (de) | 1992-06-25 |
| ATE76512T1 (de) | 1992-06-15 |
| US6391634B1 (en) | 2002-05-21 |
| IE872041L (en) | 1988-01-29 |
| GB8717792D0 (en) | 1987-09-03 |
| AU7626787A (en) | 1988-02-04 |
| ZA875551B (en) | 1988-04-27 |
| IE59984B1 (en) | 1994-05-04 |
| GB2195343A (en) | 1988-04-07 |
| EP0255342A1 (en) | 1988-02-03 |
| ES2032447T3 (es) | 1993-02-16 |
| EP0255342B1 (en) | 1992-05-20 |
| DK392387A (da) | 1988-02-12 |
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