JPH0586933B2 - - Google Patents
Info
- Publication number
- JPH0586933B2 JPH0586933B2 JP61196347A JP19634786A JPH0586933B2 JP H0586933 B2 JPH0586933 B2 JP H0586933B2 JP 61196347 A JP61196347 A JP 61196347A JP 19634786 A JP19634786 A JP 19634786A JP H0586933 B2 JPH0586933 B2 JP H0586933B2
- Authority
- JP
- Japan
- Prior art keywords
- bbi
- chymase
- inhibitors
- inhibitor
- degranulation
- 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
- 210000003630 histaminocyte Anatomy 0.000 claims description 17
- 239000003112 inhibitor Substances 0.000 claims description 17
- 235000010469 Glycine max Nutrition 0.000 claims description 14
- 244000068988 Glycine max Species 0.000 claims description 14
- 239000002753 trypsin inhibitor Substances 0.000 claims description 6
- 229940122618 Trypsin inhibitor Drugs 0.000 claims description 4
- 101710162629 Trypsin inhibitor Proteins 0.000 claims description 4
- 239000004480 active ingredient Substances 0.000 claims description 2
- 108090000227 Chymases Proteins 0.000 description 15
- 102000003858 Chymases Human genes 0.000 description 15
- 108060005989 Tryptase Proteins 0.000 description 9
- 102000001400 Tryptase Human genes 0.000 description 9
- 230000000694 effects Effects 0.000 description 9
- 230000002401 inhibitory effect Effects 0.000 description 8
- 238000000034 method Methods 0.000 description 8
- NTYJJOPFIAHURM-UHFFFAOYSA-N Histamine Chemical compound NCCC1=CN=CN1 NTYJJOPFIAHURM-UHFFFAOYSA-N 0.000 description 7
- 210000004027 cell Anatomy 0.000 description 6
- 239000008187 granular material Substances 0.000 description 6
- 235000018102 proteins Nutrition 0.000 description 6
- 102000004169 proteins and genes Human genes 0.000 description 6
- 108090000623 proteins and genes Proteins 0.000 description 6
- 230000005764 inhibitory process Effects 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- MRXDGVXSWIXTQL-HYHFHBMOSA-N (2s)-2-[[(1s)-1-(2-amino-1,4,5,6-tetrahydropyrimidin-6-yl)-2-[[(2s)-4-methyl-1-oxo-1-[[(2s)-1-oxo-3-phenylpropan-2-yl]amino]pentan-2-yl]amino]-2-oxoethyl]carbamoylamino]-3-phenylpropanoic acid Chemical compound C([C@H](NC(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C=O)C1NC(N)=NCC1)C(O)=O)C1=CC=CC=C1 MRXDGVXSWIXTQL-HYHFHBMOSA-N 0.000 description 3
- OLVPQBGMUGIKIW-UHFFFAOYSA-N Chymostatin Natural products C=1C=CC=CC=1CC(C=O)NC(=O)C(C(C)CC)NC(=O)C(C1NC(N)=NCC1)NC(=O)NC(C(O)=O)CC1=CC=CC=C1 OLVPQBGMUGIKIW-UHFFFAOYSA-N 0.000 description 3
- 206010061218 Inflammation Diseases 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 241000700159 Rattus Species 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 108010086192 chymostatin Proteins 0.000 description 3
- 229960001340 histamine Drugs 0.000 description 3
- 230000004054 inflammatory process Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- DIOSHTLNZVXJOF-UHFFFAOYSA-N 2,5-bis(3-oxobutanoylamino)benzenesulfonic acid Chemical compound CC(=O)CC(=O)NC1=CC=C(NC(=O)CC(C)=O)C(S(O)(=O)=O)=C1 DIOSHTLNZVXJOF-UHFFFAOYSA-N 0.000 description 2
- 101710202338 Bowman-Birk type trypsin inhibitor Proteins 0.000 description 2
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 2
- 206010020751 Hypersensitivity Diseases 0.000 description 2
- 108090000190 Thrombin 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
- 230000009471 action Effects 0.000 description 2
- -1 aliphatic ketones Chemical class 0.000 description 2
- 208000026935 allergic disease Diseases 0.000 description 2
- 239000003601 chymase inhibitor Substances 0.000 description 2
- 239000012043 crude product Substances 0.000 description 2
- 238000009792 diffusion process Methods 0.000 description 2
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 238000005342 ion exchange Methods 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 229960004072 thrombin Drugs 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 1
- PRCSBHBEAWPOAV-UHFFFAOYSA-N 2-(benzylamino)-5-(diaminomethylideneamino)-n-(4-nitrophenyl)pentanamide Chemical compound C=1C=C([N+]([O-])=O)C=CC=1NC(=O)C(CCCN=C(N)N)NCC1=CC=CC=C1 PRCSBHBEAWPOAV-UHFFFAOYSA-N 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 206010010744 Conjunctivitis allergic Diseases 0.000 description 1
- 235000019750 Crude protein Nutrition 0.000 description 1
- GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 208000004262 Food Hypersensitivity Diseases 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 241001126260 Nippostrongylus Species 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 206010039085 Rhinitis allergic Diseases 0.000 description 1
- 108010073771 Soybean Proteins Proteins 0.000 description 1
- 208000024780 Urticaria Diseases 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 201000009961 allergic asthma Diseases 0.000 description 1
- 208000002205 allergic conjunctivitis Diseases 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- 230000009285 allergic inflammation Effects 0.000 description 1
- 201000010105 allergic rhinitis Diseases 0.000 description 1
- 201000010435 allergic urticaria Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 208000024998 atopic conjunctivitis Diseases 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- 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 1
- 235000021240 caseins Nutrition 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 239000003541 chymotrypsin inhibitor Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- YQDHCCVUYCIGSW-LBPRGKRZSA-N ethyl (2s)-2-benzamido-5-(diaminomethylideneamino)pentanoate Chemical group NC(=N)NCCC[C@@H](C(=O)OCC)NC(=O)C1=CC=CC=C1 YQDHCCVUYCIGSW-LBPRGKRZSA-N 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 235000020932 food allergy Nutrition 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 210000004379 membrane Anatomy 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 230000008560 physiological behavior Effects 0.000 description 1
- 239000003495 polar organic solvent Substances 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 238000009938 salting Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 235000019710 soybean protein Nutrition 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 125000002730 succinyl group Chemical group C(CCC(=O)*)(=O)* 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 239000002750 tryptase inhibitor Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Plant Substances (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61196347A JPS6351335A (ja) | 1986-08-20 | 1986-08-20 | 肥満細胞脱顆粒抑制剤 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP61196347A JPS6351335A (ja) | 1986-08-20 | 1986-08-20 | 肥満細胞脱顆粒抑制剤 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS6351335A JPS6351335A (ja) | 1988-03-04 |
| JPH0586933B2 true JPH0586933B2 (en:Method) | 1993-12-14 |
Family
ID=16356325
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP61196347A Granted JPS6351335A (ja) | 1986-08-20 | 1986-08-20 | 肥満細胞脱顆粒抑制剤 |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS6351335A (en:Method) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU6782494A (en) * | 1993-04-30 | 1994-11-21 | Lxr Biotechnology Inc. | Methods of identifying potentially therapeutically effective agents and cell strains for use therein |
| TW492975B (en) * | 1993-07-26 | 2002-07-01 | Novartis Ag | Tryptase inhibitor |
| US5759548A (en) * | 1993-11-30 | 1998-06-02 | Lxr Biotechnology Inc. | Compositions which inhibit apoptosis, methods of purifying the compositions and uses thereof |
| US5620888A (en) * | 1994-12-29 | 1997-04-15 | Lxr Biotechnology, Inc. | Cell strains for use in identifying potentially therapeutically effective agents |
| US5614198A (en) * | 1995-07-25 | 1997-03-25 | The Trustees Of The University Of Pennsylvania | Bowman-Birk Inhibitor compositions for treatment of inflammatory disease |
| JPH11512439A (ja) * | 1995-09-14 | 1999-10-26 | エルエックスアール バイオテクノロジー インコーポレイテッド | リン脂質の混合物を含む抗アポトーシス活性を有する組成物 |
| US6495532B1 (en) | 1997-03-19 | 2002-12-17 | Sky High, Llc | Compositions containing lysophosphotidic acids which inhibit apoptosis and uses thereof |
| US6949528B1 (en) | 1998-03-18 | 2005-09-27 | Goddard John G | Compositions containing lysophosphatidic acids which inhibit apoptosis and uses thereof |
| DE60126199T2 (de) | 2000-02-22 | 2008-02-28 | Asubio Pharma Co., Ltd. | Therapeutische behandlung von eosinophilie durch verwendung von chymase-inhibitoren als aktive bestandteile |
| WO2009060915A1 (ja) * | 2007-11-06 | 2009-05-14 | San-Ei Gen F.F.I., Inc. | 唾液分泌促進剤 |
| KR102688761B1 (ko) * | 2016-03-03 | 2024-07-29 | 호유 가부시키가이샤 | 대두 알레르기의 항원 |
| CN108700574B (zh) * | 2016-03-03 | 2022-07-15 | 朋友股份有限公司 | 大豆变态反应的抗原 |
-
1986
- 1986-08-20 JP JP61196347A patent/JPS6351335A/ja active Granted
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6351335A (ja) | 1988-03-04 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| LAPS | Cancellation because of no payment of annual fees |