JPH01300893A - ヒトカリクレイン様蛋白質の産生方法 - Google Patents
ヒトカリクレイン様蛋白質の産生方法Info
- Publication number
- JPH01300893A JPH01300893A JP12962988A JP12962988A JPH01300893A JP H01300893 A JPH01300893 A JP H01300893A JP 12962988 A JP12962988 A JP 12962988A JP 12962988 A JP12962988 A JP 12962988A JP H01300893 A JPH01300893 A JP H01300893A
- Authority
- JP
- Japan
- Prior art keywords
- human kallikrein
- kallikrein
- protein
- human
- plasmid
- 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.)
- Granted
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 34
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 30
- 230000001689 kallikreinlike Effects 0.000 title claims abstract description 29
- 238000004519 manufacturing process Methods 0.000 title claims description 7
- 102000001399 Kallikrein Human genes 0.000 claims abstract description 45
- 108060005987 Kallikrein Proteins 0.000 claims abstract description 45
- 230000001766 physiological effect Effects 0.000 claims abstract description 7
- 239000013604 expression vector Substances 0.000 claims description 13
- 239000000126 substance Substances 0.000 claims description 12
- 239000013612 plasmid Substances 0.000 abstract description 27
- 239000012634 fragment Substances 0.000 abstract description 23
- 241000588724 Escherichia coli Species 0.000 abstract description 12
- 244000005700 microbiome Species 0.000 abstract description 5
- 241000894006 Bacteria Species 0.000 abstract description 4
- 239000013598 vector Substances 0.000 abstract description 4
- 206010020772 Hypertension Diseases 0.000 abstract description 3
- 239000001963 growth medium Substances 0.000 abstract 1
- 230000003248 secreting effect Effects 0.000 abstract 1
- 238000002560 therapeutic procedure Methods 0.000 abstract 1
- 108020004414 DNA Proteins 0.000 description 25
- 102000004190 Enzymes Human genes 0.000 description 13
- 108090000790 Enzymes Proteins 0.000 description 13
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 12
- 239000000872 buffer Substances 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- 238000007796 conventional method Methods 0.000 description 8
- 230000000694 effects Effects 0.000 description 7
- 238000000034 method Methods 0.000 description 7
- 108010076504 Protein Sorting Signals Proteins 0.000 description 6
- 239000007864 aqueous solution Substances 0.000 description 6
- 210000004027 cell Anatomy 0.000 description 6
- 239000002299 complementary DNA Substances 0.000 description 6
- 238000010438 heat treatment Methods 0.000 description 6
- 229910001629 magnesium chloride Inorganic materials 0.000 description 6
- 239000000203 mixture Substances 0.000 description 6
- 210000000496 pancreas Anatomy 0.000 description 6
- 238000005119 centrifugation Methods 0.000 description 5
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- 108091027305 Heteroduplex Proteins 0.000 description 4
- 108010093008 Kinins Proteins 0.000 description 4
- 102000002397 Kinins Human genes 0.000 description 4
- 102000003827 Plasma Kallikrein Human genes 0.000 description 4
- 108090000113 Plasma Kallikrein Proteins 0.000 description 4
- 150000001413 amino acids Chemical group 0.000 description 4
- 239000007853 buffer solution Substances 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 208000035475 disorder Diseases 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- UEGPKNKPLBYCNK-UHFFFAOYSA-L magnesium acetate Chemical compound [Mg+2].CC([O-])=O.CC([O-])=O UEGPKNKPLBYCNK-UHFFFAOYSA-L 0.000 description 4
- 239000011654 magnesium acetate Substances 0.000 description 4
- 229940069446 magnesium acetate Drugs 0.000 description 4
- 235000011285 magnesium acetate Nutrition 0.000 description 4
- SCVFZCLFOSHCOH-UHFFFAOYSA-M potassium acetate Chemical compound [K+].CC([O-])=O SCVFZCLFOSHCOH-UHFFFAOYSA-M 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 210000002700 urine Anatomy 0.000 description 4
- 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 3
- 102000012410 DNA Ligases Human genes 0.000 description 3
- 108010061982 DNA Ligases Proteins 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 3
- 230000026731 phosphorylation Effects 0.000 description 3
- 238000006366 phosphorylation reaction Methods 0.000 description 3
- 238000013518 transcription Methods 0.000 description 3
- 230000035897 transcription Effects 0.000 description 3
- 239000001226 triphosphate Substances 0.000 description 3
- 235000011178 triphosphate Nutrition 0.000 description 3
- 239000012588 trypsin Substances 0.000 description 3
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 description 2
- 241000282472 Canis lupus familiaris Species 0.000 description 2
- 206010065559 Cerebral arteriosclerosis Diseases 0.000 description 2
- 241000766026 Coregonus nasus Species 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 108010024636 Glutathione Proteins 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 102000010631 Kininogens Human genes 0.000 description 2
- 108010077861 Kininogens Proteins 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 208000002720 Malnutrition Diseases 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108700006385 OmpF Proteins 0.000 description 2
- 101710116435 Outer membrane protein Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 2
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 2
- 208000025865 Ulcer Diseases 0.000 description 2
- 206010052428 Wound Diseases 0.000 description 2
- 208000027418 Wounds and injury Diseases 0.000 description 2
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 230000017531 blood circulation Effects 0.000 description 2
- 230000036772 blood pressure Effects 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 2
- 229960005542 ethidium bromide Drugs 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 2
- 239000000411 inducer Substances 0.000 description 2
- 201000005851 intracranial arteriosclerosis Diseases 0.000 description 2
- 230000001071 malnutrition Effects 0.000 description 2
- 235000000824 malnutrition Nutrition 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 208000015380 nutritional deficiency disease Diseases 0.000 description 2
- 235000011056 potassium acetate Nutrition 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 230000016160 smooth muscle contraction Effects 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 2
- 231100000397 ulcer Toxicity 0.000 description 2
- 230000008728 vascular permeability Effects 0.000 description 2
- 230000024883 vasodilation Effects 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- URNKXHHGSVKUKV-HJOGWXRNSA-N (2s)-n-[(2s)-1-[[(2s)-5-(diaminomethylideneamino)-2-[(4-methyl-2-oxochromen-7-yl)amino]pentanoyl]amino]-1-oxo-3-phenylpropan-2-yl]pyrrolidine-2-carboxamide Chemical compound C([C@@H](C(=O)NC(=O)[C@H](CCCN=C(N)N)NC1=CC=2OC(=O)C=C(C=2C=C1)C)NC(=O)[C@H]1NCCC1)C1=CC=CC=C1 URNKXHHGSVKUKV-HJOGWXRNSA-N 0.000 description 1
- KDRNOBUWMVLVFH-UHFFFAOYSA-N 2-methyl-n-(2,2,6,6-tetramethylpiperidin-4-yl)prop-2-enamide Chemical compound CC(=C)C(=O)NC1CC(C)(C)NC(C)(C)C1 KDRNOBUWMVLVFH-UHFFFAOYSA-N 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
- 239000005695 Ammonium acetate Substances 0.000 description 1
- 108020004638 Circular DNA Proteins 0.000 description 1
- 206010011224 Cough Diseases 0.000 description 1
- 238000007400 DNA extraction Methods 0.000 description 1
- 108050009160 DNA polymerase 1 Proteins 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- 108010053070 Glutathione Disulfide Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000740112 Homo sapiens Membrane-associated transporter protein Proteins 0.000 description 1
- 101000578940 Homo sapiens PDZ domain-containing protein MAGIX Proteins 0.000 description 1
- 102100037258 Membrane-associated transporter protein Human genes 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 1
- 108700028353 OmpC Proteins 0.000 description 1
- 102100028326 PDZ domain-containing protein MAGIX Human genes 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 108020005091 Replication Origin Proteins 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-N acetic acid Substances CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 235000019257 ammonium acetate Nutrition 0.000 description 1
- 229940043376 ammonium acetate Drugs 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000011536 extraction buffer Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 229960004198 guanidine Drugs 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- 230000001965 increasing effect Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- UOEFDXYUEPHESS-QMGXLNLGSA-N isopropyl beta-D-galactopyranoside Chemical compound CC(C)O[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O UOEFDXYUEPHESS-QMGXLNLGSA-N 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- PZLXYMQOCNYUIO-UHFFFAOYSA-N lithium;hydrochloride Chemical compound [Li].Cl PZLXYMQOCNYUIO-UHFFFAOYSA-N 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000002715 modification method Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 108010084493 preprokallikrein Proteins 0.000 description 1
- 108010028105 prolyl-phenylalanyl-arginine-4-methylcoumaryl-7-amide Proteins 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 235000019333 sodium laurylsulphate Nutrition 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000013076 target substance Substances 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- PIEPQKCYPFFYMG-UHFFFAOYSA-N tris acetate Chemical compound CC(O)=O.OCC(N)(CO)CO PIEPQKCYPFFYMG-UHFFFAOYSA-N 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP12962988A JPH01300893A (ja) | 1988-05-27 | 1988-05-27 | ヒトカリクレイン様蛋白質の産生方法 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP12962988A JPH01300893A (ja) | 1988-05-27 | 1988-05-27 | ヒトカリクレイン様蛋白質の産生方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH01300893A true JPH01300893A (ja) | 1989-12-05 |
| JPH0448432B2 JPH0448432B2 (enExample) | 1992-08-06 |
Family
ID=15014219
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP12962988A Granted JPH01300893A (ja) | 1988-05-27 | 1988-05-27 | ヒトカリクレイン様蛋白質の産生方法 |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH01300893A (enExample) |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS61265092A (ja) * | 1985-05-18 | 1986-11-22 | Mitsubishi Chem Ind Ltd | 発現用ベクタ−、これを用いる蛋白の産生方法及び該ベクタ−で形質転換された宿主 |
| JPS62126980A (ja) * | 1985-11-26 | 1987-06-09 | Shigetada Nakanishi | Ｄｎａ断片 |
-
1988
- 1988-05-27 JP JP12962988A patent/JPH01300893A/ja active Granted
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS61265092A (ja) * | 1985-05-18 | 1986-11-22 | Mitsubishi Chem Ind Ltd | 発現用ベクタ−、これを用いる蛋白の産生方法及び該ベクタ−で形質転換された宿主 |
| JPS62126980A (ja) * | 1985-11-26 | 1987-06-09 | Shigetada Nakanishi | Ｄｎａ断片 |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH0448432B2 (enExample) | 1992-08-06 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| LAPS | Cancellation because of no payment of annual fees |