DE69219440T2 - Endothelin-konvertierende Enzyme - Google Patents
Endothelin-konvertierende EnzymeInfo
- Publication number
- DE69219440T2 DE69219440T2 DE69219440T DE69219440T DE69219440T2 DE 69219440 T2 DE69219440 T2 DE 69219440T2 DE 69219440 T DE69219440 T DE 69219440T DE 69219440 T DE69219440 T DE 69219440T DE 69219440 T2 DE69219440 T2 DE 69219440T2
- Authority
- DE
- Germany
- Prior art keywords
- endothelin
- density
- converting enzyme
- centrifuging
- converting
- 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
- 102000048186 Endothelin-converting enzyme 1 Human genes 0.000 title claims description 119
- 108030001679 Endothelin-converting enzyme 1 Proteins 0.000 title claims description 119
- 102100033902 Endothelin-1 Human genes 0.000 claims description 64
- 101800004490 Endothelin-1 Proteins 0.000 claims description 64
- 238000005119 centrifugation Methods 0.000 claims description 53
- 230000000694 effects Effects 0.000 claims description 51
- 102000003965 Endothelin-2 Human genes 0.000 claims description 48
- 108090000387 Endothelin-2 Proteins 0.000 claims description 48
- 102100029109 Endothelin-3 Human genes 0.000 claims description 48
- 108010072844 Endothelin-3 Proteins 0.000 claims description 48
- ZGOVYTPSWMLYOF-QEADGSHQSA-N chembl1790180 Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(O)=O)NC(=O)[C@H]1NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](CC=2C=CC(O)=CC=2)NC(=O)[C@H](C(C)C)NC(=O)[C@H]2CSSC[C@@H](C(N[C@H](CC=3C=CC=CC=3)C(=O)N[C@H](C(=O)N[C@H](CCC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N2)[C@H](C)O)=O)NC(=O)[C@@H]([C@@H](C)O)NC(=O)[C@H](N)CSSC1)C1=CNC=N1 ZGOVYTPSWMLYOF-QEADGSHQSA-N 0.000 claims description 48
- MLFJHYIHIKEBTQ-IYRKOGFYSA-N endothelin 2 Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(O)=O)NC(=O)[C@H]1NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@H](C(C)C)NC(=O)[C@@H]2CSSC[C@@H](C(N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=3C4=CC=CC=C4NC=3)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N2)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CSSC1)C1=CNC=N1 MLFJHYIHIKEBTQ-IYRKOGFYSA-N 0.000 claims description 48
- 238000000034 method Methods 0.000 claims description 35
- 210000004369 blood Anatomy 0.000 claims description 32
- 239000008280 blood Substances 0.000 claims description 32
- 239000006228 supernatant Substances 0.000 claims description 30
- 238000000926 separation method Methods 0.000 claims description 25
- 210000002966 serum Anatomy 0.000 claims description 24
- 239000000872 buffer Substances 0.000 claims description 21
- 210000002381 plasma Anatomy 0.000 claims description 19
- 238000006243 chemical reaction Methods 0.000 claims description 18
- 210000000056 organ Anatomy 0.000 claims description 16
- 210000002826 placenta Anatomy 0.000 claims description 16
- 210000001519 tissue Anatomy 0.000 claims description 15
- 238000004440 column chromatography Methods 0.000 claims description 12
- 210000004962 mammalian cell Anatomy 0.000 claims description 10
- 238000002523 gelfiltration Methods 0.000 claims description 9
- 241000124008 Mammalia Species 0.000 claims 1
- 239000000243 solution Substances 0.000 description 51
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 36
- IOLCXVTUBQKXJR-UHFFFAOYSA-M potassium bromide Chemical compound [K+].[Br-] IOLCXVTUBQKXJR-UHFFFAOYSA-M 0.000 description 34
- 102000002045 Endothelin Human genes 0.000 description 25
- 108050009340 Endothelin Proteins 0.000 description 25
- ZUBDGKVDJUIMQQ-UBFCDGJISA-N endothelin-1 Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(O)=O)NC(=O)[C@H]1NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@@H](CC=2C=CC(O)=CC=2)NC(=O)[C@H](C(C)C)NC(=O)[C@H]2CSSC[C@@H](C(N[C@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)N2)=O)NC(=O)[C@@H](CO)NC(=O)[C@H](N)CSSC1)C1=CNC=N1 ZUBDGKVDJUIMQQ-UBFCDGJISA-N 0.000 description 25
- 102000004190 Enzymes Human genes 0.000 description 19
- 108090000790 Enzymes Proteins 0.000 description 19
- 238000004519 manufacturing process Methods 0.000 description 17
- 239000011780 sodium chloride Substances 0.000 description 17
- 239000012475 sodium chloride buffer Substances 0.000 description 16
- 239000002904 solvent Substances 0.000 description 16
- 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 10
- 102000004895 Lipoproteins Human genes 0.000 description 10
- 108090001030 Lipoproteins Proteins 0.000 description 10
- 239000003480 eluent Substances 0.000 description 10
- 229940071106 ethylenediaminetetraacetate Drugs 0.000 description 10
- 239000003112 inhibitor Substances 0.000 description 9
- 239000000203 mixture Substances 0.000 description 9
- 239000002245 particle Substances 0.000 description 8
- 210000000172 cytosol Anatomy 0.000 description 7
- 238000000502 dialysis Methods 0.000 description 7
- 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 6
- 210000003918 fraction a Anatomy 0.000 description 6
- 238000001962 electrophoresis Methods 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- DGEZNRSVGBDHLK-UHFFFAOYSA-N [1,10]phenanthroline Chemical compound C1=CN=C2C3=NC=CC=C3C=CC2=C1 DGEZNRSVGBDHLK-UHFFFAOYSA-N 0.000 description 4
- 238000002156 mixing Methods 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 239000007858 starting material Substances 0.000 description 4
- 241000283690 Bos taurus Species 0.000 description 3
- 229910021380 Manganese Chloride Inorganic materials 0.000 description 3
- GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 229960002685 biotin Drugs 0.000 description 3
- 235000020958 biotin Nutrition 0.000 description 3
- 239000011616 biotin Substances 0.000 description 3
- 210000004556 brain Anatomy 0.000 description 3
- 210000004027 cell Anatomy 0.000 description 3
- 229960000633 dextran sulfate Drugs 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 238000006911 enzymatic reaction Methods 0.000 description 3
- 210000002196 fr. b Anatomy 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 210000004185 liver Anatomy 0.000 description 3
- 239000011565 manganese chloride Substances 0.000 description 3
- 235000002867 manganese chloride Nutrition 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 102000006734 Beta-Globulins Human genes 0.000 description 2
- 108010087504 Beta-Globulins Proteins 0.000 description 2
- 206010009192 Circulatory collapse Diseases 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 206010020772 Hypertension Diseases 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 229920005654 Sephadex Polymers 0.000 description 2
- 239000012507 Sephadex™ Substances 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 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 description 2
- 208000006673 asthma Diseases 0.000 description 2
- 230000002490 cerebral effect Effects 0.000 description 2
- 238000012790 confirmation Methods 0.000 description 2
- 210000004748 cultured cell Anatomy 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 208000019622 heart disease Diseases 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 210000000936 intestine Anatomy 0.000 description 2
- 230000000302 ischemic effect Effects 0.000 description 2
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 208000017169 kidney disease Diseases 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 206010040560 shock Diseases 0.000 description 2
- 210000000813 small intestine Anatomy 0.000 description 2
- 239000012086 standard solution Substances 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- IHPYMWDTONKSCO-UHFFFAOYSA-N 2,2'-piperazine-1,4-diylbisethanesulfonic acid Chemical compound OS(=O)(=O)CCN1CCN(CCS(O)(=O)=O)CC1 IHPYMWDTONKSCO-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-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
- 206010002383 Angina Pectoris Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 208000014644 Brain disease Diseases 0.000 description 1
- 241000743293 Cellana mazatlandica Species 0.000 description 1
- 208000018152 Cerebral disease Diseases 0.000 description 1
- 206010008190 Cerebrovascular accident Diseases 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 206010019280 Heart failures Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 239000007990 PIPES buffer Substances 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 208000006011 Stroke Diseases 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 206010047139 Vasoconstriction Diseases 0.000 description 1
- 230000001919 adrenal effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 206010003119 arrhythmia Diseases 0.000 description 1
- 230000006793 arrhythmia Effects 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 239000007982 barbital buffer Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 230000036765 blood level Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 230000002517 constrictor effect Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- MQRJBSHKWOFOGF-UHFFFAOYSA-L disodium;carbonate;hydrate Chemical compound O.[Na+].[Na+].[O-]C([O-])=O MQRJBSHKWOFOGF-UHFFFAOYSA-L 0.000 description 1
- 210000003038 endothelium Anatomy 0.000 description 1
- 210000003989 endothelium vascular Anatomy 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 102000034238 globular proteins Human genes 0.000 description 1
- 108091005896 globular proteins Proteins 0.000 description 1
- 239000012456 homogeneous solution Substances 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- -1 hypertension Chemical compound 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 208000023589 ischemic disease Diseases 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 230000005923 long-lasting effect Effects 0.000 description 1
- 229940099607 manganese chloride Drugs 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 201000008383 nephritis Diseases 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000011321 prophylaxis Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 210000002345 respiratory system Anatomy 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- BHZOKUMUHVTPBX-UHFFFAOYSA-M sodium acetic acid acetate Chemical compound [Na+].CC(O)=O.CC([O-])=O BHZOKUMUHVTPBX-UHFFFAOYSA-M 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 210000003437 trachea Anatomy 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 210000004509 vascular smooth muscle cell Anatomy 0.000 description 1
- 230000025033 vasoconstriction Effects 0.000 description 1
- 239000005526 vasoconstrictor agent Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6489—Metalloendopeptidases (3.4.24)
- C12N9/6497—Endothelin-converting enzyme (3.4.24.71)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/24—Metalloendopeptidases (3.4.24)
- C12Y304/24071—Endothelin-converting enzyme 1 (3.4.24.71)
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP31687491 | 1991-11-29 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DE69219440D1 DE69219440D1 (de) | 1997-06-05 |
| DE69219440T2 true DE69219440T2 (de) | 1997-08-07 |
Family
ID=18081879
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE69219440T Expired - Fee Related DE69219440T2 (de) | 1991-11-29 | 1992-11-30 | Endothelin-konvertierende Enzyme |
Country Status (3)
| Country | Link |
|---|---|
| US (1) | US5462869A (OSRAM) |
| EP (1) | EP0545344B1 (OSRAM) |
| DE (1) | DE69219440T2 (OSRAM) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0638643A1 (en) * | 1993-08-13 | 1995-02-15 | Nisshin Flour Milling Co., Ltd. | Endothelin converting enzymes and processes for preparing them |
| US6063592A (en) * | 1998-11-13 | 2000-05-16 | New York Blood Center, Inc. | Kell protein proteolytic activity |
| EP1409690A2 (en) | 1999-09-24 | 2004-04-21 | Lexicon Genetics Incorporated | Human endothelin converting enzyme-like proteins and polynucleotides encoding the same |
| US7183239B2 (en) | 2001-12-12 | 2007-02-27 | Clearwater International, Llc | Gel plugs and pigs for pipeline use |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2966939B2 (ja) * | 1990-12-07 | 1999-10-25 | 日清製粉株式会社 | ヒト細胞由来のエンドセリン変換酵素 |
| CA2100355A1 (en) * | 1991-02-04 | 1992-08-05 | Lynne H. Parker Botehlo | Endothelin converting enzyme |
-
1992
- 1992-11-30 DE DE69219440T patent/DE69219440T2/de not_active Expired - Fee Related
- 1992-11-30 EP EP92120430A patent/EP0545344B1/en not_active Expired - Lifetime
-
1994
- 1994-05-23 US US08/247,413 patent/US5462869A/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| EP0545344A2 (en) | 1993-06-09 |
| US5462869A (en) | 1995-10-31 |
| DE69219440D1 (de) | 1997-06-05 |
| EP0545344B1 (en) | 1997-05-02 |
| EP0545344A3 (OSRAM) | 1994-02-16 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| 8364 | No opposition during term of opposition | ||
| 8327 | Change in the person/name/address of the patent owner |
Owner name: NISSHIN SEIFUN GROUP INC., TOKIO/TOKYO, JP |
|
| 8339 | Ceased/non-payment of the annual fee |