NO175214B - - Google Patents
Info
- Publication number
- NO175214B NO175214B NO862100A NO862100A NO175214B NO 175214 B NO175214 B NO 175214B NO 862100 A NO862100 A NO 862100A NO 862100 A NO862100 A NO 862100A NO 175214 B NO175214 B NO 175214B
- Authority
- NO
- Norway
- Prior art keywords
- alpha
- enzyme
- enzymatic mixture
- amidating
- substrate
- Prior art date
Links
- 108090000790 Enzymes Proteins 0.000 claims abstract description 69
- 102000004190 Enzymes Human genes 0.000 claims abstract description 69
- 230000002255 enzymatic effect Effects 0.000 claims abstract description 26
- 239000000758 substrate Substances 0.000 claims abstract description 23
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 20
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 19
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 19
- 238000000034 method Methods 0.000 claims abstract description 14
- 208000037196 Medullary thyroid carcinoma Diseases 0.000 claims abstract description 13
- 208000023356 medullary thyroid gland carcinoma Diseases 0.000 claims abstract description 13
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 13
- 208000013818 thyroid gland medullary carcinoma Diseases 0.000 claims abstract description 13
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 claims abstract description 10
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims abstract description 6
- 102100039087 Peptidyl-alpha-hydroxyglycine alpha-amidating lyase Human genes 0.000 claims abstract description 5
- 235000010323 ascorbic acid Nutrition 0.000 claims abstract description 5
- 239000011668 ascorbic acid Substances 0.000 claims abstract description 5
- 108010007262 peptidylglycine monooxygenase Proteins 0.000 claims abstract description 5
- 229940072107 ascorbate Drugs 0.000 claims abstract description 4
- 239000000203 mixture Substances 0.000 claims description 26
- 230000000694 effects Effects 0.000 claims description 25
- 210000004027 cell Anatomy 0.000 claims description 17
- 238000007112 amidation reaction Methods 0.000 claims description 14
- 238000006243 chemical reaction Methods 0.000 claims description 9
- 150000001413 amino acids Chemical class 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 6
- JPVYNHNXODAKFH-UHFFFAOYSA-N Cu2+ Chemical compound [Cu+2] JPVYNHNXODAKFH-UHFFFAOYSA-N 0.000 claims description 5
- 206010028980 Neoplasm Diseases 0.000 claims description 5
- 108020004511 Recombinant DNA Proteins 0.000 claims description 5
- 239000003104 tissue culture media Substances 0.000 claims description 5
- 125000003277 amino group Chemical group 0.000 claims description 4
- 229910001431 copper ion Inorganic materials 0.000 claims description 4
- 238000001542 size-exclusion chromatography Methods 0.000 claims description 4
- 102000055006 Calcitonin Human genes 0.000 claims description 3
- 108060001064 Calcitonin Proteins 0.000 claims description 3
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical group N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 claims description 3
- 229960004015 calcitonin Drugs 0.000 claims description 3
- 238000000338 in vitro Methods 0.000 claims description 3
- 239000000126 substance Substances 0.000 claims description 3
- 102000016938 Catalase Human genes 0.000 claims description 2
- 108010053835 Catalase Proteins 0.000 claims description 2
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 claims description 2
- 238000005571 anion exchange chromatography Methods 0.000 claims description 2
- 230000015572 biosynthetic process Effects 0.000 claims description 2
- 229910001882 dioxygen Inorganic materials 0.000 claims description 2
- 238000011210 chromatographic step Methods 0.000 claims 4
- 239000003638 chemical reducing agent Substances 0.000 claims 3
- 229920002616 peptidyl amide Polymers 0.000 claims 2
- 125000001151 peptidyl group Chemical group 0.000 claims 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims 2
- 238000002305 strong-anion-exchange chromatography Methods 0.000 claims 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 claims 1
- 239000003480 eluent Substances 0.000 claims 1
- 238000010828 elution Methods 0.000 claims 1
- 230000017854 proteolysis Effects 0.000 claims 1
- 239000007858 starting material Substances 0.000 claims 1
- 238000003786 synthesis reaction Methods 0.000 claims 1
- 239000004471 Glycine Substances 0.000 abstract description 8
- 229920001184 polypeptide Polymers 0.000 abstract description 6
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 abstract description 5
- 229910052760 oxygen Inorganic materials 0.000 abstract description 5
- 239000001301 oxygen Substances 0.000 abstract description 5
- 241000894006 Bacteria Species 0.000 abstract description 3
- 239000000499 gel Substances 0.000 abstract description 3
- 229920002401 polyacrylamide Polymers 0.000 abstract description 3
- -1 Cu+2 ions Chemical class 0.000 abstract 1
- 108010093096 Immobilized Enzymes Proteins 0.000 abstract 1
- 239000000427 antigen Substances 0.000 abstract 1
- 102000036639 antigens Human genes 0.000 abstract 1
- 108091007433 antigens Proteins 0.000 abstract 1
- 229940088598 enzyme Drugs 0.000 description 47
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 14
- 241000700159 Rattus Species 0.000 description 11
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 6
- 230000009435 amidation Effects 0.000 description 5
- 230000004048 modification Effects 0.000 description 4
- 238000012986 modification Methods 0.000 description 4
- 230000001817 pituitary effect Effects 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 230000002862 amidating effect Effects 0.000 description 3
- 239000000284 extract Substances 0.000 description 3
- 230000001323 posttranslational effect Effects 0.000 description 3
- 239000011347 resin Substances 0.000 description 3
- 229920005989 resin Polymers 0.000 description 3
- 108020004414 DNA Proteins 0.000 description 2
- 206010062767 Hypophysitis Diseases 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 238000005349 anion exchange Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 239000012847 fine chemical Substances 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 210000003635 pituitary gland Anatomy 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- KETVITBYSZOWFK-RYUDHWBXSA-N (2s)-2-[[(2s)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylbutanamide Chemical compound CC(C)[C@@H](C(N)=O)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 KETVITBYSZOWFK-RYUDHWBXSA-N 0.000 description 1
- HALGLMAADGHVSV-UHFFFAOYSA-N 1-aminopropane-2-sulfonic acid Chemical compound NCC(C)S(O)(=O)=O HALGLMAADGHVSV-UHFFFAOYSA-N 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000251730 Chondrichthyes Species 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-UWTATZPHSA-N D-alanine Chemical compound C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 1
- NWEGIYMHTZXVBP-OCCSQVGLSA-N Dtyr-Val-Gly Chemical class [O-]C(=O)CNC(=O)[C@H](C(C)C)NC(=O)[C@H]([NH3+])CC1=CC=C(O)C=C1 NWEGIYMHTZXVBP-OCCSQVGLSA-N 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 239000000637 Melanocyte-Stimulating Hormone Substances 0.000 description 1
- 108010007013 Melanocyte-Stimulating Hormones Proteins 0.000 description 1
- 108010074633 Mixed Function Oxygenases Proteins 0.000 description 1
- 102000008109 Mixed Function Oxygenases Human genes 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 239000012506 Sephacryl® Substances 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 229940059260 amidate Drugs 0.000 description 1
- 150000001412 amines Chemical group 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 150000001879 copper Chemical class 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 229940108928 copper Drugs 0.000 description 1
- 229940079919 digestives enzyme preparation Drugs 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- NPUKDXXFDDZOKR-LLVKDONJSA-N etomidate Chemical compound CCOC(=O)C1=CN=CN1[C@H](C)C1=CC=CC=C1 NPUKDXXFDDZOKR-LLVKDONJSA-N 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 125000004029 hydroxymethyl group Chemical group [H]OC([H])([H])* 0.000 description 1
- 210000003016 hypothalamus Anatomy 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000000955 neuroendocrine Effects 0.000 description 1
- 230000000720 neurosecretory effect Effects 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 229920001192 peptidylglycine Polymers 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000000135 prohibitive effect Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000012609 strong anion exchange resin Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 108010037823 tyrosylvalinamide Proteins 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0071—Oxidoreductases (1.) acting on paired donors with incorporation of molecular oxygen (1.14)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- 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
- C07K14/575—Hormones
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y114/00—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14)
- C12Y114/17—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14) with reduced ascorbate as one donor, and incorporation of one atom of oxygen (1.14.17)
- C12Y114/17003—Peptidylglycine monooxygenase (1.14.17.3)
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Wood Science & Technology (AREA)
- Biophysics (AREA)
- Engineering & Computer Science (AREA)
- Gastroenterology & Hepatology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Immunology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Endocrinology (AREA)
- Toxicology (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Saccharide Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US06/655,366 US4708934A (en) | 1984-09-27 | 1984-09-27 | α-amidation enzyme |
| PCT/US1985/001616 WO1986002099A1 (en) | 1984-09-27 | 1985-08-26 | Alpha-amidation enzyme |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO862100L NO862100L (no) | 1986-05-27 |
| NO175214B true NO175214B (ja) | 1994-06-06 |
| NO175214C NO175214C (ja) | 1994-09-14 |
Family
ID=24628603
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO86862100A NO862100L (no) | 1984-09-27 | 1986-05-27 | Alfa-amideringsenzym. |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US4708934A (ja) |
| EP (1) | EP0201511B1 (ja) |
| JP (1) | JP2594037B2 (ja) |
| AT (1) | ATE92522T1 (ja) |
| CA (1) | CA1341037C (ja) |
| DE (1) | DE3587506T2 (ja) |
| DK (1) | DK241486A (ja) |
| FI (1) | FI100993B1 (ja) |
| HU (1) | HU195857B (ja) |
| LT (1) | LT2661B (ja) |
| NO (1) | NO862100L (ja) |
| RU (1) | RU1802814C (ja) |
| WO (1) | WO1986002099A1 (ja) |
Families Citing this family (48)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6319685B1 (en) * | 1984-09-27 | 2001-11-20 | Unigene Laboratories, Inc. | Alpha-amidating enzyme compositions and processes for their production and use |
| DE3612302A1 (de) * | 1986-04-11 | 1987-10-15 | Hoechst Ag | Chromophore peptide, verfahren zu ihrer herstellung und ihre verwendung zum nachweis der peptidylglycin-(alpha)-amidierenden monooxygenase |
| JPH0775541B2 (ja) * | 1986-06-07 | 1995-08-16 | 壽之 松尾 | Ｃ末端アミド化酵素及びその製造方法 |
| US5821083A (en) * | 1987-07-17 | 1998-10-13 | Suntory Limited | Recombinant C-terminal α-amidating enzyme |
| JP2598050B2 (ja) | 1987-07-17 | 1997-04-09 | サントリー株式会社 | Ｃ−末端α−アミド化酵素 |
| US5789234A (en) * | 1987-08-14 | 1998-08-04 | Unigene Laboratories, Inc. | Expression systems for amidating enzyme |
| US6255067B1 (en) * | 1987-09-15 | 2001-07-03 | The Johns Hopkins University | cDNA encoding peptidyl-glycine alpha-amidating monooxygenase (PAM) |
| JP2653820B2 (ja) * | 1988-03-14 | 1997-09-17 | 壽之 松尾 | アミド化酵素及びその製造方法 |
| WO1989012096A1 (en) * | 1988-05-30 | 1989-12-14 | Shiseido Co. Ltd. | C-terminus amidation enzyme composition, process for its preparation and its use |
| JP2512575B2 (ja) * | 1988-05-30 | 1996-07-03 | 株式会社資生堂 | Ｃ末端アミド化酵素組成物、調製方法および使用 |
| JP2845468B2 (ja) * | 1989-01-17 | 1999-01-13 | サントリー株式会社 | ヒト甲状腺由来Ｃ―末端α―アミド化酵素 |
| US5871995A (en) * | 1989-08-15 | 1999-02-16 | Shiseido Company, Ltd. | Purified enzymes participating in C-terminal amidation |
| EP0448513A3 (en) * | 1990-03-21 | 1991-12-27 | Japat Ltd | Process for production of peptidylglycine alpha-hydroxylating monooxygenase and use thereof |
| DK220890D0 (da) * | 1990-09-14 | 1990-09-14 | Ole Buchardt | Fremgangsmaade til fremstilling af c-terminalt amiderede peptider |
| US5580751A (en) * | 1990-09-14 | 1996-12-03 | Carlsberg A/S | Process for the preparation of C-terminally amidated peptides |
| JP2774769B2 (ja) * | 1993-04-26 | 1998-07-09 | 賢治 寒川 | アドレノメデュリン |
| WO1997013410A1 (en) * | 1995-10-13 | 1997-04-17 | Boston Medical Center Corporation | Hybrid molecules containing amidated polypeptide binding ligands |
| US5912014A (en) * | 1996-03-15 | 1999-06-15 | Unigene Laboratories, Inc. | Oral salmon calcitonin pharmaceutical products |
| ATE484572T1 (de) | 1997-04-16 | 2010-10-15 | Unigene Lab Inc | Direkte expression von peptiden ins kulturmedium |
| US6507788B1 (en) | 1999-02-25 | 2003-01-14 | Société de Conseils de Recherches et D'Applications Scientifiques (S.C.R.A.S.) | Rational selection of putative peptides from identified nucleotide, or peptide sequences, of unknown function |
| US8088734B2 (en) | 2003-01-21 | 2012-01-03 | Unigene Laboratories Inc. | Oral delivery of peptides |
| US7445911B2 (en) * | 2004-11-24 | 2008-11-04 | Unigene Laboratories Inc. | Enzymatic reactions in the presence of keto acids |
| DE102004058306A1 (de) * | 2004-12-01 | 2006-07-27 | Sanofi-Aventis Deutschland Gmbh | Verfahren zur Herstellung von Carboxy-terminal amidierten Peptiden |
| PA8660701A1 (es) | 2005-02-04 | 2006-09-22 | Pfizer Prod Inc | Agonistas de pyy y sus usos |
| CA2613471C (en) * | 2005-06-24 | 2016-09-06 | Unigene Laboratories, Inc. | Cell lines for expressing enzyme useful in the preparation of amidated products |
| US8377863B2 (en) | 2007-05-29 | 2013-02-19 | Unigene Laboratories Inc. | Peptide pharmaceutical for oral delivery |
| JP5401312B2 (ja) * | 2007-06-29 | 2014-01-29 | 第一三共株式会社 | 組換えＣ−末端α−アミド化酵素誘導体 |
| CN102292346B (zh) | 2009-01-22 | 2015-12-02 | 关键生物科学有限公司 | 肥胖的治疗 |
| US9096843B2 (en) | 2009-12-01 | 2015-08-04 | Novo Nordisk A/S | Peptidyl α-hydroxyglycine α-amidating lyases |
| TW201138808A (en) | 2010-05-03 | 2011-11-16 | Bristol Myers Squibb Co | Serum albumin binding molecules |
| US9102753B2 (en) | 2011-06-15 | 2015-08-11 | Ugp Therapeutics, Inc. | Anti-inflammatory pharmaceutical products |
| US9533022B2 (en) | 2011-11-02 | 2017-01-03 | KeyBioscience A/S | Peptide analogs for treating diseases and disorders |
| AU2012332265B2 (en) | 2011-11-02 | 2016-11-10 | Keybioscience Ag | Peptide analogs for treating diseases and disorders |
| EP3095484B1 (en) | 2011-11-02 | 2018-05-02 | KeyBioscience AG | Calcitonin mimetics for treating diseases and disorders |
| EP3321278B1 (en) | 2013-11-14 | 2019-01-09 | KeyBioscience AG | Calcitonin mimetics for treating diseases and disorders |
| WO2015084875A1 (en) | 2013-12-02 | 2015-06-11 | Stealth Peptides International, Inc. | Compositions and methods for treating vitiligo |
| WO2015183988A1 (en) | 2014-05-28 | 2015-12-03 | Stealth Peptides International, Inc. | Therapeutic compositions including therapeutic small molecules and uses thereof |
| EP3148565A4 (en) | 2014-05-28 | 2018-06-06 | Stealth Biotherapeutics Corp | Therapeutic compositions including frataxin, lactoferrin, and mitochondrial energy generating enzymes, and uses thereof |
| WO2015195737A1 (en) | 2014-06-17 | 2015-12-23 | Stealth Peptides International, Inc. | Methods of identifying and monitoring mitochondrial dysfunction using monocyte screening |
| GB201500263D0 (en) | 2015-01-08 | 2015-02-25 | Keybioscience Ag | Calcitonin analogues for treating diseases and disorders |
| US9833411B2 (en) | 2015-01-12 | 2017-12-05 | Enteris Biopharma, Inc. | Solid oral dosage forms |
| WO2016130899A1 (en) | 2015-02-13 | 2016-08-18 | The Board Of Trustees Of The University Of Illinois | Peptide inhibition of ccr3-mediated diseases or conditions |
| GB201704429D0 (en) | 2017-03-21 | 2017-05-03 | Keybioscience Ag | Calcitonin mimetics for treating diseases and disorders |
| GB201707955D0 (en) | 2017-05-18 | 2017-07-05 | Keybioscience Ag | Dual amylin and calcitonin receptor agonists for treating diseases and disorders |
| GB201813677D0 (en) | 2018-08-22 | 2018-10-03 | Keybioscience Ag | Calcitonin mimetics for treating diseases and disorders |
| GB201813678D0 (en) | 2018-08-22 | 2018-10-03 | Keybioscience Ag | Acylated calcitonin mimetics |
| EP4003393A1 (en) | 2019-07-29 | 2022-06-01 | The Board Of Trustees Of The University Of Illinois | Composition and method for promoting wound healing |
| GB202001024D0 (en) | 2020-01-24 | 2020-03-11 | Key Bioscience Ag | Oxyntomodulin mimetics |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6319685B1 (en) * | 1984-09-27 | 2001-11-20 | Unigene Laboratories, Inc. | Alpha-amidating enzyme compositions and processes for their production and use |
-
1984
- 1984-09-27 US US06/655,366 patent/US4708934A/en not_active Expired - Lifetime
-
1985
- 1985-08-26 WO PCT/US1985/001616 patent/WO1986002099A1/en not_active Application Discontinuation
- 1985-08-26 EP EP85904514A patent/EP0201511B1/en not_active Revoked
- 1985-08-26 HU HU853879A patent/HU195857B/hu not_active IP Right Cessation
- 1985-08-26 JP JP60503976A patent/JP2594037B2/ja not_active Expired - Lifetime
- 1985-08-26 AT AT85904514T patent/ATE92522T1/de not_active IP Right Cessation
- 1985-08-26 DE DE85904514T patent/DE3587506T2/de not_active Revoked
- 1985-09-25 CA CA000491512A patent/CA1341037C/en not_active Expired - Lifetime
-
1986
- 1986-05-23 DK DK241486A patent/DK241486A/da not_active Application Discontinuation
- 1986-05-26 FI FI862216A patent/FI100993B1/fi not_active IP Right Cessation
- 1986-05-26 RU SU864027596A patent/RU1802814C/ru active
- 1986-05-27 NO NO86862100A patent/NO862100L/no not_active IP Right Cessation
-
1993
- 1993-09-27 LT LTRP1130A patent/LT2661B/xx not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| AU594026B2 (en) | 1990-03-01 |
| DE3587506T2 (de) | 1994-01-13 |
| DE3587506D1 (en) | 1993-09-09 |
| EP0201511A1 (en) | 1986-11-20 |
| WO1986002099A1 (en) | 1986-04-10 |
| AU4802785A (en) | 1986-04-17 |
| EP0201511A4 (en) | 1988-05-31 |
| US4708934A (en) | 1987-11-24 |
| DK241486D0 (da) | 1986-05-23 |
| HU195857B (en) | 1988-07-28 |
| NO862100L (no) | 1986-05-27 |
| DK241486A (da) | 1986-05-23 |
| HUT41444A (en) | 1987-04-28 |
| JP2594037B2 (ja) | 1997-03-26 |
| FI94361C (fi) | 1995-08-25 |
| CA1341037C (en) | 2000-06-27 |
| FI862216A0 (fi) | 1986-05-26 |
| LT2661B (lt) | 1994-04-25 |
| FI100993B1 (fi) | 1998-03-31 |
| ATE92522T1 (de) | 1993-08-15 |
| FI862216A (fi) | 1986-05-26 |
| FI94361B (fi) | 1995-05-15 |
| EP0201511B1 (en) | 1993-08-04 |
| NO175214C (ja) | 1994-09-14 |
| JPS62500560A (ja) | 1987-03-12 |
| RU1802814C (ru) | 1993-03-15 |
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