JPH0669370B2 - モノクローナル抗ウシラクトフェリン抗体産生ハイブリドーマの製造法 - Google Patents
モノクローナル抗ウシラクトフェリン抗体産生ハイブリドーマの製造法Info
- Publication number
- JPH0669370B2 JPH0669370B2 JP59145667A JP14566784A JPH0669370B2 JP H0669370 B2 JPH0669370 B2 JP H0669370B2 JP 59145667 A JP59145667 A JP 59145667A JP 14566784 A JP14566784 A JP 14566784A JP H0669370 B2 JPH0669370 B2 JP H0669370B2
- Authority
- JP
- Japan
- Prior art keywords
- bovine lactoferrin
- producing
- lactoferrin
- hybridoma
- bovine
- Prior art date
- 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 - Fee Related
Links
- 210000004408 hybridoma Anatomy 0.000 title claims description 42
- 229940072440 bovine lactoferrin Drugs 0.000 title claims description 40
- 238000004519 manufacturing process Methods 0.000 title claims description 5
- 101000798100 Bos taurus Lactotransferrin Proteins 0.000 claims description 29
- 210000004027 cell Anatomy 0.000 claims description 21
- 238000000034 method Methods 0.000 claims description 16
- 230000004927 fusion Effects 0.000 claims description 15
- 210000000952 spleen Anatomy 0.000 claims description 12
- 238000002649 immunization Methods 0.000 claims description 11
- 230000003053 immunization Effects 0.000 claims description 11
- 210000004698 lymphocyte Anatomy 0.000 claims description 8
- 206010035226 Plasma cell myeloma Diseases 0.000 claims description 7
- 201000000050 myeloid neoplasm Diseases 0.000 claims description 7
- 239000002202 Polyethylene glycol Substances 0.000 claims description 6
- 229920001223 polyethylene glycol Polymers 0.000 claims description 6
- 239000002671 adjuvant Substances 0.000 claims description 5
- 239000000839 emulsion Substances 0.000 claims description 5
- 238000003113 dilution method Methods 0.000 claims description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 17
- 108010063045 Lactoferrin Proteins 0.000 description 14
- 102000010445 Lactoferrin Human genes 0.000 description 14
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 description 14
- 229940078795 lactoferrin Drugs 0.000 description 14
- 235000021242 lactoferrin Nutrition 0.000 description 14
- 239000002609 medium Substances 0.000 description 11
- 235000013336 milk Nutrition 0.000 description 9
- 239000008267 milk Substances 0.000 description 9
- 210000004080 milk Anatomy 0.000 description 9
- 108060003951 Immunoglobulin Proteins 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 7
- 102000018358 immunoglobulin Human genes 0.000 description 7
- 241000283690 Bos taurus Species 0.000 description 6
- 102000036639 antigens Human genes 0.000 description 6
- 108091007433 antigens Proteins 0.000 description 6
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 5
- 241000699670 Mus sp. Species 0.000 description 5
- 239000000427 antigen Substances 0.000 description 5
- 239000003456 ion exchange resin Substances 0.000 description 5
- 229920003303 ion-exchange polymer Polymers 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 4
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 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 description 4
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 238000010532 solid phase synthesis reaction Methods 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 210000004988 splenocyte Anatomy 0.000 description 4
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 3
- 101000798114 Homo sapiens Lactotransferrin Proteins 0.000 description 3
- 102000014171 Milk Proteins Human genes 0.000 description 3
- 108010011756 Milk Proteins Proteins 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 230000001332 colony forming effect Effects 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 102000050459 human LTF Human genes 0.000 description 3
- 239000012535 impurity Substances 0.000 description 3
- 235000021239 milk protein Nutrition 0.000 description 3
- 239000008055 phosphate buffer solution Substances 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 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 description 2
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 2
- 102000008133 Iron-Binding Proteins Human genes 0.000 description 2
- 108010035210 Iron-Binding Proteins Proteins 0.000 description 2
- 239000005862 Whey Substances 0.000 description 2
- 102000007544 Whey Proteins Human genes 0.000 description 2
- 108010046377 Whey Proteins Proteins 0.000 description 2
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 239000001569 carbon dioxide Substances 0.000 description 2
- 229910002092 carbon dioxide Inorganic materials 0.000 description 2
- 239000005018 casein Substances 0.000 description 2
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 2
- 235000021240 caseins Nutrition 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 230000005757 colony formation Effects 0.000 description 2
- 210000003022 colostrum Anatomy 0.000 description 2
- 235000021277 colostrum Nutrition 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000004817 gas chromatography Methods 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 230000003393 splenic effect Effects 0.000 description 2
- 229940104230 thymidine Drugs 0.000 description 2
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 101100203650 Bos taurus SP2 gene Proteins 0.000 description 1
- 101150096672 CEL1 gene Proteins 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 1
- 240000000279 Emilia sonchifolia Species 0.000 description 1
- 235000002139 Emilia sonchifolia Nutrition 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 238000007792 addition Methods 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 229960003896 aminopterin Drugs 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
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 230000002924 anti-infective effect Effects 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 230000003385 bacteriostatic effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000007500 overflow downdraw method Methods 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 231100000572 poisoning Toxicity 0.000 description 1
- 230000000607 poisoning effect Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000001568 sexual effect Effects 0.000 description 1
- 235000020183 skimmed milk Nutrition 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/79—Transferrins, e.g. lactoferrins, ovotransferrins
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Immunology (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)
Priority Applications (6)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP59145667A JPH0669370B2 (ja) | 1984-07-13 | 1984-07-13 | モノクローナル抗ウシラクトフェリン抗体産生ハイブリドーマの製造法 |
NZ212690A NZ212690A (en) | 1984-07-13 | 1985-07-09 | Hybridoma capable of producing monoclonal antibody against bovine lactoferrin |
DE19853524585 DE3524585A1 (de) | 1984-07-13 | 1985-07-10 | Zur erzeugung eines monoklonalen antikoerpers gegen bovines lactoferrin faehiges hybridoma |
FR8510745A FR2567539B1 (fr) | 1984-07-13 | 1985-07-12 | Hybridome capable de produire un anticorps monoclonal contre la lactoferrine bovine et procede pour sa preparation |
BE0/215340A BE902877A (fr) | 1984-07-13 | 1985-07-12 | Hybridome capable de produire un anticorps monoclonal vis-a-vis de la lactoferrine bovine |
GB08517597A GB2162856B (en) | 1984-07-13 | 1985-07-12 | Hybridoma capable of producing a monoclonal antibody against bovine lactoferrin |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP59145667A JPH0669370B2 (ja) | 1984-07-13 | 1984-07-13 | モノクローナル抗ウシラクトフェリン抗体産生ハイブリドーマの製造法 |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS6125482A JPS6125482A (ja) | 1986-02-04 |
JPH0669370B2 true JPH0669370B2 (ja) | 1994-09-07 |
Family
ID=15390298
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP59145667A Expired - Fee Related JPH0669370B2 (ja) | 1984-07-13 | 1984-07-13 | モノクローナル抗ウシラクトフェリン抗体産生ハイブリドーマの製造法 |
Country Status (6)
Country | Link |
---|---|
JP (1) | JPH0669370B2 (enrdf_load_stackoverflow) |
BE (1) | BE902877A (enrdf_load_stackoverflow) |
DE (1) | DE3524585A1 (enrdf_load_stackoverflow) |
FR (1) | FR2567539B1 (enrdf_load_stackoverflow) |
GB (1) | GB2162856B (enrdf_load_stackoverflow) |
NZ (1) | NZ212690A (enrdf_load_stackoverflow) |
Families Citing this family (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS61145200A (ja) * | 1984-12-19 | 1986-07-02 | Snow Brand Milk Prod Co Ltd | ウシラクトフェリンの分離精製法 |
JP4847406B2 (ja) * | 2007-07-11 | 2011-12-28 | 株式会社くろがね工作所 | 引戸枠の連結装置 |
JP2016540235A (ja) * | 2013-11-17 | 2016-12-22 | ニュー プロテインテック インク. | クロマトグラフィーの材料の調製法 |
-
1984
- 1984-07-13 JP JP59145667A patent/JPH0669370B2/ja not_active Expired - Fee Related
-
1985
- 1985-07-09 NZ NZ212690A patent/NZ212690A/xx unknown
- 1985-07-10 DE DE19853524585 patent/DE3524585A1/de active Granted
- 1985-07-12 BE BE0/215340A patent/BE902877A/fr not_active IP Right Cessation
- 1985-07-12 GB GB08517597A patent/GB2162856B/en not_active Expired
- 1985-07-12 FR FR8510745A patent/FR2567539B1/fr not_active Expired
Non-Patent Citations (2)
Title |
---|
BiochimicaetBiophysicaActa,446,214−225(1976) |
Nature,256,495−497(1975) |
Also Published As
Publication number | Publication date |
---|---|
DE3524585C2 (enrdf_load_stackoverflow) | 1987-09-03 |
GB2162856A (en) | 1986-02-12 |
FR2567539B1 (fr) | 1988-11-25 |
BE902877A (fr) | 1985-11-04 |
JPS6125482A (ja) | 1986-02-04 |
FR2567539A1 (fr) | 1986-01-17 |
DE3524585A1 (de) | 1986-01-16 |
GB8517597D0 (en) | 1985-08-21 |
GB2162856B (en) | 1988-03-09 |
NZ212690A (en) | 1989-01-27 |
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Legal Events
Date | Code | Title | Description |
---|---|---|---|
LAPS | Cancellation because of no payment of annual fees |