JPH0336516B2 - - Google Patents
Info
- Publication number
- JPH0336516B2 JPH0336516B2 JP60233371A JP23337185A JPH0336516B2 JP H0336516 B2 JPH0336516 B2 JP H0336516B2 JP 60233371 A JP60233371 A JP 60233371A JP 23337185 A JP23337185 A JP 23337185A JP H0336516 B2 JPH0336516 B2 JP H0336516B2
- Authority
- JP
- Japan
- Prior art keywords
- dna
- ecor
- plasmid
- site
- bamh
- 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 - Lifetime
Links
- 239000013612 plasmid Substances 0.000 claims description 58
- 108020004414 DNA Proteins 0.000 claims description 55
- 101000702488 Rattus norvegicus High affinity cationic amino acid transporter 1 Proteins 0.000 claims description 44
- 108010051210 beta-Fructofuranosidase Proteins 0.000 claims description 25
- 239000001573 invertase Substances 0.000 claims description 10
- 235000011073 invertase Nutrition 0.000 claims description 10
- 238000011144 upstream manufacturing Methods 0.000 claims description 6
- 101150014136 SUC2 gene Proteins 0.000 claims description 4
- 150000001413 amino acids Chemical class 0.000 claims description 4
- 108020004705 Codon Proteins 0.000 claims description 3
- 108091081024 Start codon Proteins 0.000 claims description 3
- 238000013519 translation Methods 0.000 claims description 2
- 239000012634 fragment Substances 0.000 description 51
- 108010065511 Amylases Proteins 0.000 description 20
- 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 14
- 238000002360 preparation method Methods 0.000 description 13
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 12
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 12
- 210000004027 cell Anatomy 0.000 description 12
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 11
- 239000000872 buffer Substances 0.000 description 11
- 102000013142 Amylases Human genes 0.000 description 10
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 10
- 101710163881 5,6-dihydroxyindole-2-carboxylic acid oxidase Proteins 0.000 description 9
- 102100030310 5,6-dihydroxyindole-2-carboxylic acid oxidase Human genes 0.000 description 9
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 9
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 239000004382 Amylase Substances 0.000 description 8
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 8
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 8
- 235000019418 amylase Nutrition 0.000 description 8
- 238000005520 cutting process Methods 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- 241000588724 Escherichia coli Species 0.000 description 7
- 108010076504 Protein Sorting Signals Proteins 0.000 description 7
- 239000007984 Tris EDTA buffer Substances 0.000 description 7
- 230000001580 bacterial effect Effects 0.000 description 7
- 239000002609 medium Substances 0.000 description 7
- 238000000034 method Methods 0.000 description 7
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 239000002244 precipitate Substances 0.000 description 6
- 108090000623 proteins and genes Proteins 0.000 description 6
- 101100163849 Arabidopsis thaliana ARS1 gene Proteins 0.000 description 5
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 5
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 5
- 101100097319 Schizosaccharomyces pombe (strain 972 / ATCC 24843) ala1 gene Proteins 0.000 description 5
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 5
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 5
- 108091008146 restriction endonucleases Proteins 0.000 description 5
- 101710163270 Nuclease Proteins 0.000 description 4
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 239000000284 extract Substances 0.000 description 4
- 229910001629 magnesium chloride Inorganic materials 0.000 description 4
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 4
- 235000019341 magnesium sulphate Nutrition 0.000 description 4
- 230000010076 replication Effects 0.000 description 4
- 150000003839 salts Chemical class 0.000 description 4
- 229920006395 saturated elastomer Polymers 0.000 description 4
- 239000001632 sodium acetate Substances 0.000 description 4
- 235000017281 sodium acetate Nutrition 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 229920001817 Agar Polymers 0.000 description 3
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 3
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 3
- 102000012410 DNA Ligases Human genes 0.000 description 3
- 108010061982 DNA Ligases Proteins 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 239000008272 agar Substances 0.000 description 3
- 244000309466 calf Species 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- 238000010276 construction Methods 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 238000012869 ethanol precipitation Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 210000000813 small intestine Anatomy 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 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 2
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 101000708578 Milk vetch dwarf virus (isolate N) Para-Rep C3 Proteins 0.000 description 2
- 108010014251 Muramidase Proteins 0.000 description 2
- 102000016943 Muramidase Human genes 0.000 description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 229920002472 Starch Polymers 0.000 description 2
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 239000002131 composite material Substances 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 125000001475 halogen functional group Chemical group 0.000 description 2
- 239000005457 ice water Substances 0.000 description 2
- 238000007169 ligase reaction Methods 0.000 description 2
- XIXADJRWDQXREU-UHFFFAOYSA-M lithium acetate Chemical compound [Li+].CC([O-])=O XIXADJRWDQXREU-UHFFFAOYSA-M 0.000 description 2
- 239000004325 lysozyme Substances 0.000 description 2
- 229960000274 lysozyme Drugs 0.000 description 2
- 235000010335 lysozyme Nutrition 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 239000013606 secretion vector Substances 0.000 description 2
- 239000013605 shuttle vector Substances 0.000 description 2
- ATHGHQPFGPMSJY-UHFFFAOYSA-N spermidine Chemical compound NCCCCNCCCN ATHGHQPFGPMSJY-UHFFFAOYSA-N 0.000 description 2
- 239000008107 starch Substances 0.000 description 2
- 235000019698 starch Nutrition 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 101150072109 trr1 gene Proteins 0.000 description 2
- JIAARYAFYJHUJI-UHFFFAOYSA-L zinc dichloride Chemical compound [Cl-].[Cl-].[Zn+2] JIAARYAFYJHUJI-UHFFFAOYSA-L 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- ZKHQWZAMYRWXGA-KQYNXXCUSA-J ATP(4-) Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-J 0.000 description 1
- ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 description 1
- 102000004594 DNA Polymerase I Human genes 0.000 description 1
- 108010017826 DNA Polymerase I Proteins 0.000 description 1
- 230000004543 DNA replication Effects 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- 108020005091 Replication Origin Proteins 0.000 description 1
- 101150006914 TRP1 gene Proteins 0.000 description 1
- TTWYZDPBDWHJOR-IDIVVRGQSA-L adenosine triphosphate disodium Chemical compound [Na+].[Na+].C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O TTWYZDPBDWHJOR-IDIVVRGQSA-L 0.000 description 1
- 125000003275 alpha amino acid group Chemical group 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 239000010410 layer Substances 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229940057838 polyethylene glycol 4000 Drugs 0.000 description 1
- 229940093429 polyethylene glycol 6000 Drugs 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 229940063673 spermidine Drugs 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 239000002344 surface layer Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- 239000011592 zinc chloride Substances 0.000 description 1
- 235000005074 zinc chloride Nutrition 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
- C12N15/625—DNA sequences coding for fusion proteins containing a sequence coding for a signal sequence
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
- C12N15/81—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence
Landscapes
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Chemical & Material Sciences (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Physics & Mathematics (AREA)
- Mycology (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP60233371A JPS6296086A (ja) | 1985-10-21 | 1985-10-21 | 複合プラスミド |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP60233371A JPS6296086A (ja) | 1985-10-21 | 1985-10-21 | 複合プラスミド |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS6296086A JPS6296086A (ja) | 1987-05-02 |
| JPH0336516B2 true JPH0336516B2 (fr) | 1991-05-31 |
Family
ID=16954072
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP60233371A Granted JPS6296086A (ja) | 1985-10-21 | 1985-10-21 | 複合プラスミド |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS6296086A (fr) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003060071A2 (fr) | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Proteines hybrides d'albumine |
| WO2009058322A1 (fr) | 2007-10-31 | 2009-05-07 | Human Genome Sciences, Inc. | Protéines de fusion d'albumine |
| EP2090589A1 (fr) | 2002-02-07 | 2009-08-19 | Dyax Corp. | Peptides de domaine de Kunitz fusionnées à l'albumine |
Families Citing this family (25)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH02156881A (ja) * | 1988-12-12 | 1990-06-15 | Agency Of Ind Science & Technol | サッカロマイセスセレビシエｐｏｐ２ |
| JPH02156880A (ja) * | 1988-12-12 | 1990-06-15 | Agency Of Ind Science & Technol | サッカロマイセスセレビシエｐｏｐ１ |
| US5629167A (en) | 1994-04-19 | 1997-05-13 | Biocine S.P.A. | Detection of antibodies against Chlamydia trachomatis pgp3 antigen in patient sera by enzyme-linked immunosorbent assay |
| GB9526733D0 (en) | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| BR9813930A (pt) | 1997-11-06 | 2006-12-19 | Chiron Spa | antìgeno neisserial |
| AU1979599A (en) | 1998-01-14 | 1999-08-02 | Chiron S.P.A. | (neisseria meningitidis) antigens |
| GB9808932D0 (en) | 1998-04-27 | 1998-06-24 | Chiron Spa | Polyepitope carrier protein |
| CN101293920B (zh) | 1998-05-01 | 2012-07-18 | 诺华疫苗和诊断公司 | 脑膜炎奈瑟球菌抗原和组合物 |
| BR0010130A (pt) | 1999-04-30 | 2002-06-04 | Chiron Spa | Antìgenos de neisseria conservados |
| GB9911683D0 (en) | 1999-05-19 | 1999-07-21 | Chiron Spa | Antigenic peptides |
| GB9916529D0 (en) | 1999-07-14 | 1999-09-15 | Chiron Spa | Antigenic peptides |
| MXPA02004283A (es) | 1999-10-29 | 2002-10-17 | Chiron Spa | Peptidos antigenicos neisseriales. |
| BRPI0107679B8 (pt) | 2000-01-17 | 2021-05-25 | Chiron Spa | composição compreendendo vesículas de membrana externa do grupo sérico b de neisseria meningitidis e um componente inorgânico e uso da mesma |
| US20030171267A1 (en) | 2000-04-12 | 2003-09-11 | Rosen Craig A. | Albumin fusion proteins |
| DE60139563D1 (de) | 2000-10-27 | 2009-09-24 | Craig J Venter Inst Inc | Nukleinsäuren und proteine von gruppen a und b-streptokokken |
| GB0107658D0 (en) | 2001-03-27 | 2001-05-16 | Chiron Spa | Streptococcus pneumoniae |
| GB0107661D0 (en) | 2001-03-27 | 2001-05-16 | Chiron Spa | Staphylococcus aureus |
| EP2335724A1 (fr) | 2001-12-12 | 2011-06-22 | Novartis Vaccines and Diagnostics S.r.l. | Immunisation contre la Chlamydia trachomatis |
| CA2506318C (fr) | 2002-11-15 | 2011-07-12 | Chiron Srl | Proteines de surface inattendues sur le meningocoque |
| US20100015168A1 (en) | 2006-06-09 | 2010-01-21 | Novartis Ag | Immunogenic compositions for streptococcus agalactiae |
| EP2054437A2 (fr) | 2006-08-07 | 2009-05-06 | Teva Biopharmaceuticals USA, Inc. | Protéines de fusion d'albumine et d'insuline |
| AU2012222833B2 (en) | 2011-03-03 | 2017-03-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design and constructs |
| WO2014012082A2 (fr) | 2012-07-13 | 2014-01-16 | Zymeworks Inc. | Conception d'échafaudages hétéromultimères et produits de recombinaison |
| CA2874083C (fr) | 2014-12-05 | 2024-01-02 | Universite Laval | Polypeptides liant le tdp-43 utiles pour le traitement de maladies neurodegeneratives |
| CN107400636B (zh) * | 2017-08-10 | 2020-10-09 | 安徽大学 | 一种蔗糖酶基因及其表达与应用 |
-
1985
- 1985-10-21 JP JP60233371A patent/JPS6296086A/ja active Granted
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003060071A2 (fr) | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Proteines hybrides d'albumine |
| EP2090589A1 (fr) | 2002-02-07 | 2009-08-19 | Dyax Corp. | Peptides de domaine de Kunitz fusionnées à l'albumine |
| WO2009058322A1 (fr) | 2007-10-31 | 2009-05-07 | Human Genome Sciences, Inc. | Protéines de fusion d'albumine |
Also Published As
| Publication number | Publication date |
|---|---|
| JPS6296086A (ja) | 1987-05-02 |
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