JPH0123447B2 - - Google Patents
Info
- Publication number
- JPH0123447B2 JPH0123447B2 JP57103777A JP10377782A JPH0123447B2 JP H0123447 B2 JPH0123447 B2 JP H0123447B2 JP 57103777 A JP57103777 A JP 57103777A JP 10377782 A JP10377782 A JP 10377782A JP H0123447 B2 JPH0123447 B2 JP H0123447B2
- Authority
- JP
- Japan
- Prior art keywords
- lpf
- activity
- pertussis
- subunit
- protein
- 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
Links
- 102000004169 proteins and genes Human genes 0.000 claims description 43
- 108090000623 proteins and genes Proteins 0.000 claims description 43
- 230000000694 effects Effects 0.000 claims description 32
- 201000005702 Pertussis Diseases 0.000 claims description 18
- 238000000034 method Methods 0.000 claims description 17
- 208000015181 infectious disease Diseases 0.000 claims description 13
- 239000000203 mixture Substances 0.000 claims description 13
- NTYJJOPFIAHURM-UHFFFAOYSA-N Histamine Chemical compound NCCC1=CN=CN1 NTYJJOPFIAHURM-UHFFFAOYSA-N 0.000 claims description 10
- 229940122199 Insulin secretagogue Drugs 0.000 claims description 8
- 108010081690 Pertussis Toxin Proteins 0.000 claims description 7
- 150000001413 amino acids Chemical class 0.000 claims description 7
- 206010024378 leukocytosis Diseases 0.000 claims description 6
- 101710194807 Protective antigen Proteins 0.000 claims description 5
- 229930006000 Sucrose Natural products 0.000 claims description 5
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 claims description 5
- 229960001340 histamine Drugs 0.000 claims description 5
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 claims description 5
- 230000001235 sensitizing effect Effects 0.000 claims description 5
- 239000005720 sucrose Substances 0.000 claims description 5
- 239000008363 phosphate buffer Substances 0.000 description 20
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 18
- 239000000243 solution Substances 0.000 description 13
- 229920002401 polyacrylamide Polymers 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- 229960005486 vaccine Drugs 0.000 description 10
- 239000004202 carbamide Substances 0.000 description 9
- 238000001962 electrophoresis Methods 0.000 description 9
- 239000002609 medium Substances 0.000 description 9
- 241000894006 Bacteria Species 0.000 description 8
- 241000588832 Bordetella pertussis Species 0.000 description 8
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 8
- 241000699670 Mus sp. Species 0.000 description 6
- 229920002684 Sepharose Polymers 0.000 description 6
- 210000000265 leukocyte Anatomy 0.000 description 6
- 230000000890 antigenic effect Effects 0.000 description 5
- 238000002523 gelfiltration Methods 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 210000004027 cell Anatomy 0.000 description 4
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 4
- 230000004083 survival effect Effects 0.000 description 4
- 239000003053 toxin Substances 0.000 description 4
- 231100000765 toxin Toxicity 0.000 description 4
- 108700012359 toxins Proteins 0.000 description 4
- 239000012506 Sephacryl® Substances 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 230000003472 neutralizing effect Effects 0.000 description 3
- ZNNZYHKDIALBAK-UHFFFAOYSA-M potassium thiocyanate Chemical compound [K+].[S-]C#N ZNNZYHKDIALBAK-UHFFFAOYSA-M 0.000 description 3
- 210000003462 vein Anatomy 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 108010038061 Chymotrypsinogen Proteins 0.000 description 2
- 229920000858 Cyclodextrin Polymers 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 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
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 229960000583 acetic acid Drugs 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000036760 body temperature Effects 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 238000012136 culture method Methods 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 239000002158 endotoxin Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- 239000012362 glacial acetic acid Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 239000002054 inoculum Substances 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 230000003914 insulin secretion Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 229940066827 pertussis vaccine Drugs 0.000 description 2
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- YZOUYRAONFXZSI-SBHWVFSVSA-N (1S,3R,5R,6R,8R,10R,11R,13R,15R,16R,18R,20R,21R,23R,25R,26R,28R,30R,31S,33R,35R,36R,37S,38R,39S,40R,41S,42R,43S,44R,45S,46R,47S,48R,49S)-5,10,15,20,25,30,35-heptakis(hydroxymethyl)-37,39,40,41,42,43,44,45,46,47,48,49-dodecamethoxy-2,4,7,9,12,14,17,19,22,24,27,29,32,34-tetradecaoxaoctacyclo[31.2.2.23,6.28,11.213,16.218,21.223,26.228,31]nonatetracontane-36,38-diol Chemical compound O([C@@H]([C@H]([C@@H]1OC)OC)O[C@H]2[C@@H](O)[C@@H]([C@@H](O[C@@H]3[C@@H](CO)O[C@@H]([C@H]([C@@H]3O)OC)O[C@@H]3[C@@H](CO)O[C@@H]([C@H]([C@@H]3OC)OC)O[C@@H]3[C@@H](CO)O[C@@H]([C@H]([C@@H]3OC)OC)O[C@@H]3[C@@H](CO)O[C@@H]([C@H]([C@@H]3OC)OC)O3)O[C@@H]2CO)OC)[C@H](CO)[C@H]1O[C@@H]1[C@@H](OC)[C@H](OC)[C@H]3[C@@H](CO)O1 YZOUYRAONFXZSI-SBHWVFSVSA-N 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 241000588807 Bordetella Species 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 102100025255 Haptoglobin Human genes 0.000 description 1
- 108050005077 Haptoglobin Proteins 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 241001510071 Pyrrhocoridae Species 0.000 description 1
- 206010049190 Red blood cell agglutination Diseases 0.000 description 1
- 102100033130 T-box transcription factor T Human genes 0.000 description 1
- 101710086566 T-box transcription factor T Proteins 0.000 description 1
- 206010043376 Tetanus Diseases 0.000 description 1
- 101710174842 Tumor necrosis factor soluble receptor Proteins 0.000 description 1
- 206010047700 Vomiting Diseases 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000004820 blood count Methods 0.000 description 1
- 239000007465 bordet-gengou-medium Substances 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 229940030156 cell vaccine Drugs 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 206010013023 diphtheria Diseases 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000003067 hemagglutinative effect Effects 0.000 description 1
- PPZMYIBUHIPZOS-UHFFFAOYSA-N histamine dihydrochloride Chemical compound Cl.Cl.NCCC1=CN=CN1 PPZMYIBUHIPZOS-UHFFFAOYSA-N 0.000 description 1
- 229960000645 histamine hydrochloride Drugs 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 231100000957 no side effect Toxicity 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 239000012466 permeate Substances 0.000 description 1
- 230000037081 physical activity Effects 0.000 description 1
- 229910052697 platinum Inorganic materials 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000012488 sample solution Substances 0.000 description 1
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 230000003068 static effect Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 229940126585 therapeutic drug Drugs 0.000 description 1
- 230000008673 vomiting Effects 0.000 description 1
Landscapes
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP57103777A JPS58222032A (ja) | 1982-06-18 | 1982-06-18 | 百日咳毒素のサブユニツト蛋白 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP57103777A JPS58222032A (ja) | 1982-06-18 | 1982-06-18 | 百日咳毒素のサブユニツト蛋白 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS58222032A JPS58222032A (ja) | 1983-12-23 |
| JPH0123447B2 true JPH0123447B2 (enrdf_load_stackoverflow) | 1989-05-02 |
Family
ID=14362860
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP57103777A Granted JPS58222032A (ja) | 1982-06-18 | 1982-06-18 | 百日咳毒素のサブユニツト蛋白 |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS58222032A (enrdf_load_stackoverflow) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE455946B (sv) * | 1986-10-20 | 1988-08-22 | Trion Forskning & Utveckling | Nya pertussistoxin-polypeptider och antigener samt testsatser, vacciner och intradermala hudtestkompositioner |
| EP0279151B1 (en) * | 1986-12-22 | 1993-04-28 | Trion Forskning- Och Utvecklings Aktiebolag | Pertussis toxin polypeptide and its uses |
| CA1337859C (en) * | 1987-04-24 | 1996-01-02 | Masashi Chazono | Method for culturing bordetella pertussis, a pertussis toxoid and a pertussis vaccine |
| JPS6485926A (en) * | 1987-06-24 | 1989-03-30 | Teijin Ltd | Mutant of bordetella pertussis |
| GB8910570D0 (en) | 1989-05-08 | 1989-06-21 | Wellcome Found | Acellular vaccine |
-
1982
- 1982-06-18 JP JP57103777A patent/JPS58222032A/ja active Granted
Also Published As
| Publication number | Publication date |
|---|---|
| JPS58222032A (ja) | 1983-12-23 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2163032C (en) | Antibody fragments in therapy | |
| Berken et al. | Properties of antibodies cytophilic for macrophages | |
| CA1231643A (en) | Composition of intravenous immune globulin | |
| AU681573B2 (en) | Type I and type II surface antigens associated with (staphylococcus epidermidis) | |
| Reiser et al. | Purification and some physicochemical properties of toxic-shock toxin | |
| EP0336736B1 (en) | Purification of pertussis toxins and production of vaccine | |
| Kim et al. | Modification of host responses to bacterial endotoxins: II. Passive transfer of immunity to bacterial endotoxin with fractions containing 19S antibodies | |
| US5667787A (en) | Purification of a pertussis outer membrane protein | |
| Amino et al. | Human lymphotoxin obtained from established lymphoid lines: purification characteristics and inhibition by anti-immunoglobulin | |
| JP2950970B2 (ja) | 百日咳菌からの６９０００ダルトンの抗原性タンパク質の精製方法 | |
| Cunningham et al. | Immunochemical properties of streptococcal M protein purified by isoelectric focusing | |
| JPH0123447B2 (enrdf_load_stackoverflow) | ||
| Rubin et al. | Specific heterologous enhancement of immune responses: V. Isolation of a soluble enhancing factor from supernatants of specifically stimulated and allogeneically induced lymphoid cells | |
| JPH0723398B2 (ja) | 初乳由来ポリペプチド因子 | |
| Geczy et al. | Antibodies to Guinea Pig Lymphokines: IV. Suppression of the Mixed Leukocyte Culture Reaction by anti-Lymphokine Globulin | |
| JPH10505356A (ja) | ヒトへの投与のための組成物および方法、抗原特異的免疫応答のダウンレギュレーションを行うことが可能なペプチド | |
| Gislason et al. | Intravenous γ-globulin infusions in patients with hypo-γ-globulinemia | |
| Chaudhry et al. | Shared and specific allergenic and antigenic components in the two sexes of American cockroach—Periplaneta americana | |
| JPH0453848B2 (enrdf_load_stackoverflow) | ||
| Maurer et al. | Immunological studies with plasma expanders derived from human plasma | |
| US6444211B2 (en) | Purification of a pertussis outer membrane protein | |
| Hall et al. | Soluble antigens of the bovine cornea | |
| Pesce et al. | Modulation of the immune response to allergens: phospholipase A degradation products suppress IgG and IgE response in mice | |
| US5324511A (en) | Vaccines and immunoglobulin G-containing preparations active against pseudomonas aeruginosa | |
| US3175947A (en) | Human serum tetanus antitoxin titer production |