CN101413009A - 一种改构的人淀粉样多肽突变体-普兰林肽(pramlintide)的制备方法 - Google Patents
一种改构的人淀粉样多肽突变体-普兰林肽(pramlintide)的制备方法 Download PDFInfo
- Publication number
- CN101413009A CN101413009A CNA2008102185331A CN200810218533A CN101413009A CN 101413009 A CN101413009 A CN 101413009A CN A2008102185331 A CNA2008102185331 A CN A2008102185331A CN 200810218533 A CN200810218533 A CN 200810218533A CN 101413009 A CN101413009 A CN 101413009A
- Authority
- CN
- China
- Prior art keywords
- tripro
- amylin
- sequence
- pramlintide
- fusion rotein
- 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
- 238000002360 preparation method Methods 0.000 title claims abstract description 15
- 229960003611 pramlintide Drugs 0.000 title claims abstract description 9
- 101001081479 Homo sapiens Islet amyloid polypeptide Proteins 0.000 title 1
- 108010029667 pramlintide Proteins 0.000 claims abstract description 43
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 39
- 230000004927 fusion Effects 0.000 claims abstract description 30
- 150000003384 small molecules Chemical class 0.000 claims abstract description 26
- 238000000034 method Methods 0.000 claims abstract description 19
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 18
- 230000014509 gene expression Effects 0.000 claims abstract description 15
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 14
- 229920001184 polypeptide Polymers 0.000 claims abstract description 13
- 241000894006 Bacteria Species 0.000 claims abstract description 7
- 238000000855 fermentation Methods 0.000 claims abstract description 6
- 230000004151 fermentation Effects 0.000 claims abstract description 6
- TZIRZGBAFTZREM-MKAGXXMWSA-N pramlintide Chemical compound C([C@@H](C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H]1NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CCCCN)CSSC1)[C@@H](C)O)C(C)C)C1=CC=CC=C1 TZIRZGBAFTZREM-MKAGXXMWSA-N 0.000 claims description 42
- 102000044159 Ubiquitin Human genes 0.000 claims description 36
- 108090000848 Ubiquitin Proteins 0.000 claims description 36
- 238000012986 modification Methods 0.000 claims description 33
- 230000004048 modification Effects 0.000 claims description 33
- 239000002773 nucleotide Substances 0.000 claims description 13
- 125000003729 nucleotide group Chemical group 0.000 claims description 13
- 239000013604 expression vector Substances 0.000 claims description 12
- 238000000746 purification Methods 0.000 claims description 11
- 241000588724 Escherichia coli Species 0.000 claims description 9
- 108020001507 fusion proteins Proteins 0.000 claims description 8
- 102000037865 fusion proteins Human genes 0.000 claims description 6
- 230000000968 intestinal effect Effects 0.000 claims description 5
- 238000012258 culturing Methods 0.000 claims description 3
- 238000003259 recombinant expression Methods 0.000 claims description 3
- 108020004705 Codon Proteins 0.000 claims 1
- 235000014304 histidine Nutrition 0.000 claims 1
- 150000002411 histidines Chemical class 0.000 claims 1
- 230000009465 prokaryotic expression Effects 0.000 claims 1
- 102000004169 proteins and genes Human genes 0.000 abstract description 12
- 230000008569 process Effects 0.000 abstract description 9
- 239000007788 liquid Substances 0.000 abstract description 3
- 241000193830 Bacillus <bacterium> Species 0.000 abstract 1
- 108700005078 Synthetic Genes Proteins 0.000 abstract 1
- 101800001117 Ubiquitin-related Proteins 0.000 abstract 1
- 210000001072 colon Anatomy 0.000 abstract 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 abstract 1
- 239000003607 modifier Substances 0.000 abstract 1
- NRKVKVQDUCJPIZ-MKAGXXMWSA-N pramlintide acetate Chemical compound C([C@@H](C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CS)NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 NRKVKVQDUCJPIZ-MKAGXXMWSA-N 0.000 abstract 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 abstract 1
- 102000004190 Enzymes Human genes 0.000 description 19
- 108090000790 Enzymes Proteins 0.000 description 19
- 102000051619 SUMO-1 Human genes 0.000 description 19
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 8
- 239000013612 plasmid Substances 0.000 description 8
- 210000004027 cell Anatomy 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 108020004414 DNA Proteins 0.000 description 6
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 6
- 239000008103 glucose Substances 0.000 description 6
- 230000007062 hydrolysis Effects 0.000 description 6
- 238000006460 hydrolysis reaction Methods 0.000 description 6
- 101000684503 Homo sapiens Sentrin-specific protease 3 Proteins 0.000 description 5
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 5
- 102100023645 Sentrin-specific protease 3 Human genes 0.000 description 5
- 235000001014 amino acid Nutrition 0.000 description 5
- 210000000496 pancreas Anatomy 0.000 description 5
- FRXSZNDVFUDTIR-UHFFFAOYSA-N 6-methoxy-1,2,3,4-tetrahydroquinoline Chemical compound N1CCCC2=CC(OC)=CC=C21 FRXSZNDVFUDTIR-UHFFFAOYSA-N 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 238000010369 molecular cloning Methods 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 3
- 108091005573 modified proteins Proteins 0.000 description 3
- 102000035118 modified proteins Human genes 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 101100539164 Caenorhabditis elegans ubc-9 gene Proteins 0.000 description 2
- 229920002101 Chitin Polymers 0.000 description 2
- 102400000321 Glucagon Human genes 0.000 description 2
- 108060003199 Glucagon Proteins 0.000 description 2
- 229920002527 Glycogen Polymers 0.000 description 2
- 108010041872 Islet Amyloid Polypeptide Proteins 0.000 description 2
- 102000036770 Islet Amyloid Polypeptide Human genes 0.000 description 2
- 102000005431 Molecular Chaperones Human genes 0.000 description 2
- 108010006519 Molecular Chaperones Proteins 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 2
- 101900335766 Saccharomyces cerevisiae Ubiquitin Proteins 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 102000002669 Small Ubiquitin-Related Modifier Proteins Human genes 0.000 description 2
- 108010043401 Small Ubiquitin-Related Modifier Proteins Proteins 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 238000005267 amalgamation Methods 0.000 description 2
- 125000000539 amino acid group Chemical group 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
- 230000004071 biological effect Effects 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000001311 chemical methods and process Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 230000005611 electricity Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 2
- 229960004666 glucagon Drugs 0.000 description 2
- 229940096919 glycogen Drugs 0.000 description 2
- 239000002054 inoculum Substances 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 230000035790 physiological processes and functions Effects 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 238000010926 purge Methods 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 210000002237 B-cell of pancreatic islet Anatomy 0.000 description 1
- 101000708016 Caenorhabditis elegans Sentrin-specific protease Proteins 0.000 description 1
- 101100008047 Caenorhabditis elegans cut-3 gene Proteins 0.000 description 1
- 101100427543 Caenorhabditis elegans ulp-2 gene Proteins 0.000 description 1
- 102000055006 Calcitonin Human genes 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- 108090000932 Calcitonin Gene-Related Peptide Proteins 0.000 description 1
- 102100025588 Calcitonin gene-related peptide 1 Human genes 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 108050008316 DNA endonuclease RBBP8 Proteins 0.000 description 1
- 102100031780 Endonuclease Human genes 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 101000693367 Homo sapiens SUMO-activating enzyme subunit 1 Proteins 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 102000015731 Peptide Hormones Human genes 0.000 description 1
- 108010038988 Peptide Hormones Proteins 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 101710180319 Protease 1 Proteins 0.000 description 1
- 102100025809 SUMO-activating enzyme subunit 1 Human genes 0.000 description 1
- 102100035250 SUMO-activating enzyme subunit 2 Human genes 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 101710081623 Small ubiquitin-related modifier 1 Proteins 0.000 description 1
- 101710137710 Thioesterase 1/protease 1/lysophospholipase L1 Proteins 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- DPDMMXDBJGCCQC-UHFFFAOYSA-N [Na].[Cl] Chemical compound [Na].[Cl] DPDMMXDBJGCCQC-UHFFFAOYSA-N 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 230000036528 appetite Effects 0.000 description 1
- 235000019789 appetite Nutrition 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 230000022131 cell cycle Effects 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 239000012295 chemical reaction liquid Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 238000013016 damping Methods 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000002641 glycemic effect Effects 0.000 description 1
- YMAWOPBAYDPSLA-UHFFFAOYSA-N glycylglycine Chemical group [NH3+]CC(=O)NCC([O-])=O YMAWOPBAYDPSLA-UHFFFAOYSA-N 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000005374 membrane filtration Methods 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000000050 nutritive effect Effects 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000026447 protein localization Effects 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 230000004960 subcellular localization Effects 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 238000010189 synthetic method Methods 0.000 description 1
- 230000017105 transposition Effects 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
Images
Landscapes
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
Description
Claims (5)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN2008102185331A CN101413009B (zh) | 2008-10-22 | 2008-10-22 | 一种改构的人淀粉样多肽突变体-普兰林肽(pramlintide)的制备方法 |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN2008102185331A CN101413009B (zh) | 2008-10-22 | 2008-10-22 | 一种改构的人淀粉样多肽突变体-普兰林肽(pramlintide)的制备方法 |
Publications (2)
Publication Number | Publication Date |
---|---|
CN101413009A true CN101413009A (zh) | 2009-04-22 |
CN101413009B CN101413009B (zh) | 2011-05-04 |
Family
ID=40593748
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CN2008102185331A Expired - Fee Related CN101413009B (zh) | 2008-10-22 | 2008-10-22 | 一种改构的人淀粉样多肽突变体-普兰林肽(pramlintide)的制备方法 |
Country Status (1)
Country | Link |
---|---|
CN (1) | CN101413009B (zh) |
Cited By (5)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101747426B (zh) * | 2009-12-18 | 2013-01-16 | 深圳翰宇药业股份有限公司 | 一种合成普兰林肽的方法 |
CN105985995A (zh) * | 2015-01-29 | 2016-10-05 | 暨南大学 | 一种利用家蚕生物反应器生产普兰林肽(pa)的方法 |
CN106554405A (zh) * | 2015-09-30 | 2017-04-05 | 深圳翰宇药业股份有限公司 | 一种多肽及其用途、制备方法 |
CN113025675A (zh) * | 2021-05-21 | 2021-06-25 | 凯莱英医药集团(天津)股份有限公司 | 多肽的制备方法 |
WO2023227133A1 (zh) * | 2022-05-27 | 2023-11-30 | 杭州先为达生物科技股份有限公司 | 人胰淀素类似物、其衍生物及用途 |
-
2008
- 2008-10-22 CN CN2008102185331A patent/CN101413009B/zh not_active Expired - Fee Related
Cited By (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN101747426B (zh) * | 2009-12-18 | 2013-01-16 | 深圳翰宇药业股份有限公司 | 一种合成普兰林肽的方法 |
CN105985995A (zh) * | 2015-01-29 | 2016-10-05 | 暨南大学 | 一种利用家蚕生物反应器生产普兰林肽(pa)的方法 |
CN106554405A (zh) * | 2015-09-30 | 2017-04-05 | 深圳翰宇药业股份有限公司 | 一种多肽及其用途、制备方法 |
CN106554405B (zh) * | 2015-09-30 | 2020-04-24 | 深圳翰宇药业股份有限公司 | 一种多肽及其用途、制备方法 |
CN113025675A (zh) * | 2021-05-21 | 2021-06-25 | 凯莱英医药集团(天津)股份有限公司 | 多肽的制备方法 |
CN113025675B (zh) * | 2021-05-21 | 2021-08-20 | 凯莱英医药集团(天津)股份有限公司 | 多肽的制备方法 |
WO2022241831A1 (zh) * | 2021-05-21 | 2022-11-24 | 凯莱英医药集团(天津)股份有限公司 | 多肽的制备方法 |
WO2023227133A1 (zh) * | 2022-05-27 | 2023-11-30 | 杭州先为达生物科技股份有限公司 | 人胰淀素类似物、其衍生物及用途 |
Also Published As
Publication number | Publication date |
---|---|
CN101413009B (zh) | 2011-05-04 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
WO2020182229A1 (zh) | 一种融合蛋白及其制备利拉鲁肽中间体多肽的方法 | |
CN103122027B (zh) | 一种重组人源胶原蛋白及其生产方法 | |
CN101413009B (zh) | 一种改构的人淀粉样多肽突变体-普兰林肽(pramlintide)的制备方法 | |
WO2021139295A1 (zh) | 一种重组多肽连接酶原及其制备、激活方法与应用 | |
JPH08333395A (ja) | ヒトプロインスリン誘導体およびヒトインスリンの製造方法 | |
CN101519446A (zh) | 一种重组人胰岛素及其类似物的制备方法 | |
CN1807456B (zh) | 重组人甲状旁腺激素pth1-34的制备方法 | |
CN110724187B (zh) | 一种高效表达利拉鲁肽前体的重组工程菌及其应用 | |
CN102839182B (zh) | 利用大肠杆菌表达系统制备重组人神经生长因子的方法 | |
CN107881187A (zh) | 将大肠杆菌表达的融合蛋白转化为利拉鲁肽的制备方法及应用 | |
CN108220315A (zh) | 一种小分子蛋白或多肽的制备方法及融合蛋白 | |
CN101144093B (zh) | 可溶性表达人ⅰ型金属硫蛋白的重组表达载体和方法 | |
CN101240033B (zh) | 一种促胰岛素分泌肽与人血清白蛋白的融合蛋白及其制备方法 | |
CN110257347B (zh) | 硫氧还蛋白突变体、其制备方法及其在重组融合蛋白生产中的应用 | |
CN106939315B (zh) | 一种草酸脱羧酶的制备方法及应用 | |
CN101967493A (zh) | 一种原核表达载体及其应用 | |
CN112522294B (zh) | 一种glp-1类似物的半重组制备方法 | |
EP3000823A1 (en) | Strong secretory signal peptide enhancing small peptide motif and use thereof | |
CN104195157A (zh) | 生物活性肽在原核细胞中的高效率重组表达和纯化方法 | |
CN114933658B (zh) | 一种短肽元件及其应用方法 | |
CN103709253A (zh) | 一种生物合成制备glp-1及其类似物的方法 | |
CN114410558A (zh) | 具有降血压功能的ace抑制肽-aceip及其基因工程制备方法 | |
CN106399340A (zh) | 一种鸡溶菌酶和鸡β‑防御素7融合基因及其制备方法 | |
CN102260697A (zh) | 融合表达重组制备人β干扰素 | |
RU2453604C1 (ru) | Гибридный белок (варианты), штамм бактерий escherichia coli - продуцент гибридного белка (варианты) и способ получения безметионинового интерферона альфа-2 человека |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
C06 | Publication | ||
PB01 | Publication | ||
C10 | Entry into substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
DD01 | Delivery of document by public notice |
Addressee: Wu Daopin Document name: Notification of an Office Action |
|
C14 | Grant of patent or utility model | ||
GR01 | Patent grant | ||
DD01 | Delivery of document by public notice |
Addressee: Guangdong Jida Genetic Pharmaceutical Engineering Research Center Co., Ltd. Document name: Notification of Passing Examination on Formalities |
|
DD01 | Delivery of document by public notice | ||
DD01 | Delivery of document by public notice |
Addressee: BIOPHARMACEUTIAL RESEARCH & DEVELOPMENT CENTER OF JINAN University Document name: Notification to Pay the Fees |
|
CP01 | Change in the name or title of a patent holder | ||
CP01 | Change in the name or title of a patent holder |
Address after: 510630 Guangdong city of Guangzhou province Tianhe District huajingxincheng Hua Jing Lu No. 37 4 floor Co-patentee after: Guangzhou Jinan University Medical Biotechnology Research and Development Center Co., Ltd Patentee after: GUANGDONG JIDA GENETIC MEDICINE ENGINEERING RESEARCH CENTER Co.,Ltd. Address before: 510630 Guangdong city of Guangzhou province Tianhe District huajingxincheng Hua Jing Lu No. 37 4 floor Co-patentee before: Medical biotechnology research and development center of Jinan University, Guangzhou Patentee before: GUANGDONG JIDA GENETIC MEDICINE ENGINEERING RESEARCH CENTER Co.,Ltd. |
|
DD01 | Delivery of document by public notice | ||
DD01 | Delivery of document by public notice |
Addressee: Person in charge of patent of Guangdong Jida gene and drug Engineering Research Center Co., Ltd Document name: Notification of Passing Examination on Formalities |
|
CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20110504 Termination date: 20191022 |
|
CF01 | Termination of patent right due to non-payment of annual fee |