JPH0476431B2 - - Google Patents

Info

Publication number: JPH0476431B2
Authority: JP; Japan
Prior art keywords: protein; antibody; antibodies; receptor group; igg
Prior art date: 1985-03-11
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired

Application number

JP4663885A

Other languages

English (en)

Japanese (ja)

Other versions

JPS61205861A (ja

Inventor

Tadashi Shudo

Juji Myauchi

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Terumo Corp

Original Assignee

Terumo Corp

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1985-03-11

Filing date

1985-03-11

Publication date

1992-12-03

1985-03-11 Application filed by Terumo Corp filed Critical Terumo Corp

1985-03-11 Priority to JP4663885A priority Critical patent/JPS61205861A/ja

1986-09-12 Publication of JPS61205861A publication Critical patent/JPS61205861A/ja

1992-12-03 Publication of JPH0476431B2 publication Critical patent/JPH0476431B2/ja

Status Granted legal-status Critical Current

Links

102000004169 proteins and genes Human genes 0.000 claims description 79
108090000623 proteins and genes Proteins 0.000 claims description 79
102000009109 Fc receptors Human genes 0.000 claims description 25
108010087819 Fc receptors Proteins 0.000 claims description 25
238000004519 manufacturing process Methods 0.000 claims description 18
230000000890 antigenic effect Effects 0.000 claims description 14
238000005406 washing Methods 0.000 claims description 9
SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical group O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 claims description 8
239000000834 fixative Substances 0.000 claims description 8
238000000034 method Methods 0.000 claims description 8
239000000872 buffer Substances 0.000 claims description 6
239000007788 liquid Substances 0.000 claims description 6
IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 claims description 3
229940027941 immunoglobulin g Drugs 0.000 description 21
101710132457 Protein A1 Proteins 0.000 description 10
210000002966 serum Anatomy 0.000 description 10
239000000243 solution Substances 0.000 description 9
229920002684 Sepharose Polymers 0.000 description 8
239000007864 aqueous solution Substances 0.000 description 8
239000002953 phosphate buffered saline Substances 0.000 description 7
241000283973 Oryctolagus cuniculus Species 0.000 description 6
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
238000001042 affinity chromatography Methods 0.000 description 5
230000000052 comparative effect Effects 0.000 description 5
230000000694 effects Effects 0.000 description 5
239000003480 eluent Substances 0.000 description 5
238000003127 radioimmunoassay Methods 0.000 description 5
230000035945 sensitivity Effects 0.000 description 5
108010058683 Immobilized Proteins Proteins 0.000 description 4
239000003463 adsorbent Substances 0.000 description 4
239000000427 antigen Substances 0.000 description 4
108091007433 antigens Proteins 0.000 description 4
102000036639 antigens Human genes 0.000 description 4
ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 4
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
241000295644 Staphylococcaceae Species 0.000 description 3
238000004587 chromatography analysis Methods 0.000 description 3
125000000524 functional group Chemical group 0.000 description 3
239000007973 glycine-HCl buffer Substances 0.000 description 3
230000003100 immobilizing effect Effects 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
241000191967 Staphylococcus aureus Species 0.000 description 2
238000002835 absorbance Methods 0.000 description 2
239000011230 binding agent Substances 0.000 description 2
238000009792 diffusion process Methods 0.000 description 2
XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
239000012634 fragment Substances 0.000 description 2
230000000951 immunodiffusion Effects 0.000 description 2
229920000642 polymer Polymers 0.000 description 2
LMDZBCPBFSXMTL-UHFFFAOYSA-N 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide Chemical compound CCN=C=NCCCN(C)C LMDZBCPBFSXMTL-UHFFFAOYSA-N 0.000 description 1
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 1
229920000936 Agarose Polymers 0.000 description 1
102000002260 Alkaline Phosphatase Human genes 0.000 description 1
108020004774 Alkaline Phosphatase Proteins 0.000 description 1
-1 CCl 3 COO - Chemical class 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
KRHYYFGTRYWZRS-UHFFFAOYSA-M Fluoride anion Chemical compound [F-] KRHYYFGTRYWZRS-UHFFFAOYSA-M 0.000 description 1
108060003951 Immunoglobulin Proteins 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
108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
206010028980 Neoplasm Diseases 0.000 description 1
108090000526 Papain Proteins 0.000 description 1
229920001213 Polysorbate 20 Polymers 0.000 description 1
239000004793 Polystyrene Substances 0.000 description 1
239000004365 Protease Substances 0.000 description 1
102000007562 Serum Albumin Human genes 0.000 description 1
108010071390 Serum Albumin Proteins 0.000 description 1
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
239000002671 adjuvant Substances 0.000 description 1
125000000539 amino acid group Chemical group 0.000 description 1
150000001413 amino acids Chemical class 0.000 description 1
229910021529 ammonia Inorganic materials 0.000 description 1
239000011324 bead Substances 0.000 description 1
201000011510 cancer Diseases 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
239000000969 carrier Substances 0.000 description 1
230000003196 chaotropic effect Effects 0.000 description 1
239000003153 chemical reaction reagent Substances 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
238000011109 contamination Methods 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
238000004132 cross linking Methods 0.000 description 1
238000001514 detection method Methods 0.000 description 1
238000010586 diagram Methods 0.000 description 1
ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 1
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 1
229940079593 drug Drugs 0.000 description 1
239000003814 drug Substances 0.000 description 1
238000010828 elution Methods 0.000 description 1
229940088598 enzyme Drugs 0.000 description 1
239000011521 glass Substances 0.000 description 1
229960004198 guanidine Drugs 0.000 description 1
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
230000008105 immune reaction Effects 0.000 description 1
230000003053 immunization Effects 0.000 description 1
238000002649 immunization Methods 0.000 description 1
238000003018 immunoassay Methods 0.000 description 1
102000018358 immunoglobulin Human genes 0.000 description 1
229960001438 immunostimulant agent Drugs 0.000 description 1
239000003022 immunostimulating agent Substances 0.000 description 1
230000003308 immunostimulating effect Effects 0.000 description 1
229910010272 inorganic material Inorganic materials 0.000 description 1
239000011147 inorganic material Substances 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
229910001629 magnesium chloride Inorganic materials 0.000 description 1
230000000873 masking effect Effects 0.000 description 1
238000005259 measurement Methods 0.000 description 1
238000004452 microanalysis Methods 0.000 description 1
239000000203 mixture Substances 0.000 description 1
238000012986 modification Methods 0.000 description 1
230000004048 modification Effects 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
229940055729 papain Drugs 0.000 description 1
235000019834 papain Nutrition 0.000 description 1
230000001717 pathogenic effect Effects 0.000 description 1
239000007981 phosphate-citrate buffer Substances 0.000 description 1
239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
229920002223 polystyrene Polymers 0.000 description 1
108090000765 processed proteins & peptides Proteins 0.000 description 1
235000019260 propionic acid Nutrition 0.000 description 1
238000011002 quantification Methods 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
238000011160 research Methods 0.000 description 1
239000000377 silicon dioxide Substances 0.000 description 1
VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 1
239000002904 solvent Substances 0.000 description 1
239000000126 substance Substances 0.000 description 1
239000000758 substrate Substances 0.000 description 1
230000001225 therapeutic 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
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/566—Immunoassay; Biospecific binding assay; Materials therefor using specific carrier or receptor proteins as ligand binding reagents where possible specific carrier or receptor proteins are classified with their target compounds
- G01N33/567—Immunoassay; Biospecific binding assay; Materials therefor using specific carrier or receptor proteins as ligand binding reagents where possible specific carrier or receptor proteins are classified with their target compounds utilising isolate of tissue or organ as binding agent

Landscapes

Health & Medical Sciences (AREA)
Engineering & Computer Science (AREA)
Life Sciences & Earth Sciences (AREA)
Biomedical Technology (AREA)
Immunology (AREA)
Molecular Biology (AREA)
Chemical & Material Sciences (AREA)
Hematology (AREA)
Urology & Nephrology (AREA)
Biotechnology (AREA)
Microbiology (AREA)
Cell Biology (AREA)
Food Science & Technology (AREA)
Medicinal Chemistry (AREA)
Physics & Mathematics (AREA)
Analytical Chemistry (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
General Physics & Mathematics (AREA)
Pathology (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Peptides Or Proteins (AREA)

JP4663885A 1985-03-11 1985-03-11 高純度抗プロテインａ抗体の製造方法 Granted JPS61205861A (ja)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
JP4663885A JPS61205861A (ja)	1985-03-11	1985-03-11	高純度抗プロテインａ抗体の製造方法

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP4663885A JPS61205861A (ja)	1985-03-11	1985-03-11	高純度抗プロテインａ抗体の製造方法

Publications (2)

Publication Number	Publication Date
JPS61205861A JPS61205861A (ja)	1986-09-12
JPH0476431B2 true JPH0476431B2 (de)	1992-12-03

Family

ID=12752844

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP4663885A Granted JPS61205861A (ja)	1985-03-11	1985-03-11	高純度抗プロテインａ抗体の製造方法

Country Status (1)

Country	Link
JP (1)	JPS61205861A (de)

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5182669A (en) *	1990-06-04	1993-01-26	Pioneer Electronic Corporation	High density optical disk and method of making

1985
- 1985-03-11 JP JP4663885A patent/JPS61205861A/ja active Granted

Also Published As

Publication number	Publication date
JPS61205861A (ja)	1986-09-12

Publication	Publication Date	Title
Inganäs et al.	1980	Interaction of human polyclonal IgE and IgG from different species with protein A from Staphylococcus aureus: demonstration of protein‐A‐reactive sites located in the Fab2 fragment of human IgG
Füglistaller	1989	Comparison of immunoglobulin binding capacities and ligand leakage using eight different protein A affinity chromatography matrices
Nisnevitch et al.	2001	The solid phase in affinity chromatography: strategies for antibody attachment
EP0391526B1 (de)	1994-11-17	Reinigungsverfahren für Antikörper
KR100249752B1 (ko)	2000-03-15	항체의특정클래스에특이적인간섭억제시약
WO1986000140A1 (en)	1986-01-03	Polyclonal antibodies, preparation and use
JPH0521510B2 (de)	1993-03-24
Doellgast et al.	1997	Sensitive assay for measurement of antibodies to Clostridium botulinum neurotoxins A, B, and E: use of hapten-labeled-antibody elution to isolate specific complexes
Lindmark et al.	1981	Quantitation of Specific IgG Antibodies in Rabbits by a Solid‐phase Radioimmunoassay with 125I‐Protein A from Staphylococcus aureus
HU179956B (en)	1983-01-28	Process for the immunological determination of antigens by means of enzyme marking
JP2681370B2 (ja)	1997-11-26	免疫測定法
Klonisch et al.	1996	Enhancement in antigen binding by a combination of synergy and antibody capture
JPH0476431B2 (de)	1992-12-03
Joshi et al.	1992	The immunochemistry of sandwich ELISAs—V. The capture antibody performance of polyclonal antibody-enriched fractions prepared by various methods
Cheng et al.	1999	Detection of IgM to hepatitis B core antigen in a reductant containing, chemiluminescence assay
JPH038512B2 (de)	1991-02-06
JP3091974B2 (ja)	2000-09-25	８―ハイドロキシ―２’―デオキシグアノシンのモノクローナル抗体及びその製造法並びにモノクローナル抗体を生産するハイブリッド細胞
JP3098970B2 (ja)	2000-10-16	タンパクのペプチド溶離免疫測定方法
JP4399115B2 (ja)	2010-01-13	天然または組換えタンパク質、ポリペプチドまたはペプチドの定量的解離の方法
US5472848A (en)	1995-12-05	Methods to aid in the diagnosis of multiple sclerosis
SU1698783A1 (ru)	1991-12-15	Способ определени антител к экзотоксину коклюшных бактерий методом иммуноферментного анализа
ES2197425T3 (es)	2004-01-01	Superficies union a ligando.
JPS6363859B2 (de)	1988-12-08
Oscarsson et al.	1991	Thiophilic adsorbents for RIA and ELISA procedures
KR910008704B1 (ko)	1991-10-19	면역학적으로 검출 가능한 물질의 측정 방법 및 이것에 적당한 반응 용기