CA2160663A1 - Methode de detection et de conversion d'un polypeptide - Google Patents
Methode de detection et de conversion d'un polypeptideInfo
- Publication number
- CA2160663A1 CA2160663A1 CA002160663A CA2160663A CA2160663A1 CA 2160663 A1 CA2160663 A1 CA 2160663A1 CA 002160663 A CA002160663 A CA 002160663A CA 2160663 A CA2160663 A CA 2160663A CA 2160663 A1 CA2160663 A1 CA 2160663A1
- Authority
- CA
- Canada
- Prior art keywords
- growth hormone
- hgh
- derivative
- rhgh
- hydrophobic
- 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.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims abstract description 24
- 108090000765 processed proteins & peptides Proteins 0.000 title abstract description 16
- 102000004196 processed proteins & peptides Human genes 0.000 title abstract description 8
- 229920001184 polypeptide Polymers 0.000 title abstract description 4
- 239000000854 Human Growth Hormone Substances 0.000 claims abstract description 69
- 108010000521 Human Growth Hormone Proteins 0.000 claims abstract description 69
- 102000002265 Human Growth Hormone Human genes 0.000 claims abstract description 69
- 239000000122 growth hormone Substances 0.000 claims abstract description 50
- 102000018997 Growth Hormone Human genes 0.000 claims abstract description 49
- 108010051696 Growth Hormone Proteins 0.000 claims abstract description 49
- 230000002209 hydrophobic effect Effects 0.000 claims abstract description 35
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims abstract description 19
- 235000018417 cysteine Nutrition 0.000 claims abstract description 17
- 238000004191 hydrophobic interaction chromatography Methods 0.000 claims abstract description 16
- -1 mercapto compound Chemical class 0.000 claims abstract description 13
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 23
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 claims description 9
- 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 claims description 6
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical group [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 claims description 5
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 claims description 5
- 108010024636 Glutathione Proteins 0.000 claims description 3
- 229960003180 glutathione Drugs 0.000 claims description 3
- 150000003839 salts Chemical class 0.000 claims description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 abstract description 5
- 229910052921 ammonium sulfate Inorganic materials 0.000 abstract description 5
- 235000011130 ammonium sulphate Nutrition 0.000 abstract description 5
- 238000010828 elution Methods 0.000 abstract description 5
- 239000001166 ammonium sulphate Substances 0.000 abstract description 4
- 238000012510 peptide mapping method Methods 0.000 abstract description 4
- 239000007983 Tris buffer Substances 0.000 description 15
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 15
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 15
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 15
- 239000012634 fragment Substances 0.000 description 13
- 108090000623 proteins and genes Proteins 0.000 description 10
- 239000000243 solution Substances 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 9
- 150000001413 amino acids Chemical class 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 238000012360 testing method Methods 0.000 description 8
- 125000000539 amino acid group Chemical group 0.000 description 7
- 238000001514 detection method Methods 0.000 description 7
- 239000012153 distilled water Substances 0.000 description 7
- 239000003480 eluent Substances 0.000 description 7
- 235000018102 proteins Nutrition 0.000 description 7
- 102000004169 proteins and genes Human genes 0.000 description 7
- 241000282414 Homo sapiens Species 0.000 description 6
- 206010062767 Hypophysitis Diseases 0.000 description 6
- 235000001014 amino acid Nutrition 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 150000001875 compounds Chemical class 0.000 description 5
- 238000004949 mass spectrometry Methods 0.000 description 5
- 210000003635 pituitary gland Anatomy 0.000 description 5
- 230000009467 reduction Effects 0.000 description 5
- 239000003643 water by type Substances 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 239000004480 active ingredient Substances 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 239000003111 growth hormone derivative Substances 0.000 description 3
- 229940121366 growth hormone derivative Drugs 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 238000010188 recombinant method Methods 0.000 description 3
- 238000004007 reversed phase HPLC Methods 0.000 description 3
- 239000002904 solvent Substances 0.000 description 3
- 239000007858 starting material Substances 0.000 description 3
- 239000012588 trypsin Substances 0.000 description 3
- 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 2
- 206010056438 Growth hormone deficiency Diseases 0.000 description 2
- 101001024703 Homo sapiens Nck-associated protein 5 Proteins 0.000 description 2
- 206010027146 Melanoderma Diseases 0.000 description 2
- 108010013127 Met-human growth hormone Proteins 0.000 description 2
- 102100036946 Nck-associated protein 5 Human genes 0.000 description 2
- 208000020221 Short stature Diseases 0.000 description 2
- 239000005864 Sulphur Substances 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000003795 desorption Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 2
- 229910000397 disodium phosphate Inorganic materials 0.000 description 2
- 235000019800 disodium phosphate Nutrition 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 239000007921 spray Substances 0.000 description 2
- 238000004885 tandem mass spectrometry Methods 0.000 description 2
- 238000013385 tryptic peptide mapping Methods 0.000 description 2
- GHKCSRZBNZQHKW-UHFFFAOYSA-N 1-sulfanylethanol Chemical compound CC(O)S GHKCSRZBNZQHKW-UHFFFAOYSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 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
- 241000972773 Aulopiformes Species 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- RWSOTUBLDIXVET-UHFFFAOYSA-N Dihydrogen sulfide Chemical compound S RWSOTUBLDIXVET-UHFFFAOYSA-N 0.000 description 1
- 206010013883 Dwarfism Diseases 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- 206010017788 Gastric haemorrhage Diseases 0.000 description 1
- JBCLFWXMTIKCCB-UHFFFAOYSA-N H-Gly-Phe-OH Natural products NCC(=O)NC(C(O)=O)CC1=CC=CC=C1 JBCLFWXMTIKCCB-UHFFFAOYSA-N 0.000 description 1
- AUIYHFRUOOKTGX-UKJIMTQDSA-N Ile-Val-Gln Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(=O)N)C(=O)O)N AUIYHFRUOOKTGX-UKJIMTQDSA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- 229920001410 Microfiber Polymers 0.000 description 1
- 208000001132 Osteoporosis Diseases 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 208000002607 Pseudarthrosis Diseases 0.000 description 1
- 241000277331 Salmonidae Species 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- RNFKSBPHLTZHLU-WHFBIAKZSA-N Ser-Cys-Gly Chemical compound C([C@@H](C(=O)N[C@@H](CS)C(=O)NCC(=O)O)N)O RNFKSBPHLTZHLU-WHFBIAKZSA-N 0.000 description 1
- BEBVVQPDSHHWQL-NRPADANISA-N Ser-Val-Glu Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O BEBVVQPDSHHWQL-NRPADANISA-N 0.000 description 1
- 208000026928 Turner syndrome Diseases 0.000 description 1
- 230000001594 aberrant effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 229940043376 ammonium acetate Drugs 0.000 description 1
- 235000019257 ammonium acetate Nutrition 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 239000008366 buffered solution Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- QHFQAJHNDKBRBO-UHFFFAOYSA-L calcium chloride hexahydrate Chemical compound O.O.O.O.O.O.[Cl-].[Cl-].[Ca+2] QHFQAJHNDKBRBO-UHFFFAOYSA-L 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 150000001793 charged compounds Chemical class 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000005227 gel permeation chromatography Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 208000000509 infertility Diseases 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 231100000535 infertility Toxicity 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000010829 isocratic elution Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 238000009940 knitting Methods 0.000 description 1
- 229940046892 lead acetate Drugs 0.000 description 1
- XCAUINMIESBTBL-UHFFFAOYSA-N lead(ii) sulfide Chemical compound [Pb]=S XCAUINMIESBTBL-UHFFFAOYSA-N 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 238000001294 liquid chromatography-tandem mass spectrometry Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 239000003658 microfiber Substances 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 230000006855 networking Effects 0.000 description 1
- 210000004789 organ system Anatomy 0.000 description 1
- 239000000825 pharmaceutical preparation Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000001817 pituitary effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 230000018406 regulation of metabolic process Effects 0.000 description 1
- 235000002020 sage Nutrition 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 210000002356 skeleton Anatomy 0.000 description 1
- 229940116591 skeleton diagnostic radiopharmaceuticals Drugs 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 230000009576 somatic growth Effects 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- PXQLVRUNWNTZOS-UHFFFAOYSA-N sulfanyl Chemical class [SH] PXQLVRUNWNTZOS-UHFFFAOYSA-N 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 210000001835 viscera Anatomy 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1133—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by redox-reactions involving cystein/cystin side chains
-
- 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
- C07K14/61—Growth hormone [GH], i.e. somatotropin
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/435—Assays involving biological materials from specific organisms or of a specific nature from animals; from humans
- G01N2333/575—Hormones
- G01N2333/61—Growth hormones [GH] (Somatotropin)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Hematology (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Urology & Nephrology (AREA)
- Organic Chemistry (AREA)
- Analytical Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Endocrinology (AREA)
- Cell Biology (AREA)
- Genetics & Genomics (AREA)
- Physics & Mathematics (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Biophysics (AREA)
- Food Science & Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK0445/93 | 1993-04-20 | ||
| DK93445A DK44593D0 (da) | 1993-04-20 | 1993-04-20 | Fremgangsmaade til fremstilling af et polypeptid |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2160663A1 true CA2160663A1 (fr) | 1994-10-27 |
Family
ID=8093625
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002160663A Abandoned CA2160663A1 (fr) | 1993-04-20 | 1994-04-19 | Methode de detection et de conversion d'un polypeptide |
Country Status (14)
| Country | Link |
|---|---|
| EP (1) | EP0695310A1 (fr) |
| JP (1) | JPH08508735A (fr) |
| KR (1) | KR960701891A (fr) |
| AU (1) | AU6535594A (fr) |
| BG (1) | BG100068A (fr) |
| CA (1) | CA2160663A1 (fr) |
| CZ (1) | CZ272895A3 (fr) |
| DK (1) | DK44593D0 (fr) |
| FI (1) | FI955000A0 (fr) |
| HU (1) | HUT73320A (fr) |
| IL (1) | IL109347A0 (fr) |
| NO (1) | NO954181L (fr) |
| PL (1) | PL311198A1 (fr) |
| WO (1) | WO1994024157A1 (fr) |
Families Citing this family (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SE9802454D0 (sv) * | 1998-07-08 | 1998-07-08 | Pharmacia & Upjohn Ab | Production of peptides |
| US20040048315A1 (en) * | 2002-08-28 | 2004-03-11 | Pharmacia Corporation | Method for the preparation of growth hormone and antagonist thereof having lower levels of isoform impurities thereof |
| CN1697839B (zh) * | 2002-08-28 | 2010-10-27 | 法玛西亚公司 | 同工型杂质水平较低的生长激素及其拮抗剂的制备方法 |
| ZA200502320B (en) * | 2002-09-20 | 2006-10-25 | Pharmacia Corp | Process for decreasing aggregate levels of pegylated protein |
| ES2337041T3 (es) * | 2002-09-20 | 2010-04-20 | Pharmacia Corporation | Procedimiento para disminuir los niveles de agregacion de proteina pegilada. |
| WO2006069940A1 (fr) | 2004-12-29 | 2006-07-06 | Novo Nordisk Health Care Ag | Procede permettant d'empecher la formation de derives trisulfures de polypeptides |
| EP2483289B1 (fr) | 2009-10-02 | 2019-03-20 | Biogen MA Inc. | Procedes permettant de detruire et de reduire la formation de liaisons trisulfure |
| EP3388443A1 (fr) | 2011-05-13 | 2018-10-17 | Biogen MA Inc. | Procédés de prévention et d'élimination des liaisons trisulfures |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4985544A (en) * | 1987-08-04 | 1991-01-15 | Kyowa Hakko Kogyo Co., Ltd. | Process for renaturing fish growth hormone |
| US5079230A (en) * | 1988-09-12 | 1992-01-07 | Pitman-Moore, Inc. | Stable bioactive somatotropins |
| ES2119779T3 (es) * | 1990-09-05 | 1998-10-16 | Southern Cross Biotech Pty Ltd | Solubilizacion de proteinas en formas activas. |
| US5151501A (en) * | 1991-12-20 | 1992-09-29 | American Cyanamid Company | Method for solubilization and naturation of somatotropins utilizing sulfolane |
-
1993
- 1993-04-20 DK DK93445A patent/DK44593D0/da not_active Application Discontinuation
-
1994
- 1994-04-19 JP JP6522643A patent/JPH08508735A/ja active Pending
- 1994-04-19 HU HU9503020A patent/HUT73320A/hu unknown
- 1994-04-19 WO PCT/DK1994/000157 patent/WO1994024157A1/fr not_active Application Discontinuation
- 1994-04-19 CZ CZ952728A patent/CZ272895A3/cs unknown
- 1994-04-19 IL IL10934794A patent/IL109347A0/xx unknown
- 1994-04-19 AU AU65355/94A patent/AU6535594A/en not_active Abandoned
- 1994-04-19 PL PL94311198A patent/PL311198A1/xx unknown
- 1994-04-19 EP EP94913048A patent/EP0695310A1/fr not_active Withdrawn
- 1994-04-19 KR KR1019950704477A patent/KR960701891A/ko not_active Application Discontinuation
- 1994-04-19 CA CA002160663A patent/CA2160663A1/fr not_active Abandoned
-
1995
- 1995-10-17 BG BG100068A patent/BG100068A/xx unknown
- 1995-10-19 NO NO954181A patent/NO954181L/no unknown
- 1995-10-19 FI FI955000A patent/FI955000A0/fi not_active Application Discontinuation
Also Published As
| Publication number | Publication date |
|---|---|
| FI955000A (fi) | 1995-10-19 |
| CZ272895A3 (en) | 1996-03-13 |
| JPH08508735A (ja) | 1996-09-17 |
| KR960701891A (ko) | 1996-03-28 |
| HU9503020D0 (en) | 1995-12-28 |
| IL109347A0 (en) | 1994-07-31 |
| FI955000A0 (fi) | 1995-10-19 |
| NO954181D0 (no) | 1995-10-19 |
| EP0695310A1 (fr) | 1996-02-07 |
| WO1994024157A1 (fr) | 1994-10-27 |
| BG100068A (en) | 1996-12-31 |
| PL311198A1 (en) | 1996-02-05 |
| AU6535594A (en) | 1994-11-08 |
| DK44593D0 (da) | 1993-04-20 |
| NO954181L (no) | 1995-10-19 |
| HUT73320A (en) | 1996-07-29 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued | ||
| FZDE | Discontinued |
Effective date: 19980420 |