SE459816B - Vektor med stark genexpression - Google Patents
Vektor med stark genexpressionInfo
- Publication number
- SE459816B SE459816B SE8303068A SE8303068A SE459816B SE 459816 B SE459816 B SE 459816B SE 8303068 A SE8303068 A SE 8303068A SE 8303068 A SE8303068 A SE 8303068A SE 459816 B SE459816 B SE 459816B
- Authority
- SE
- Sweden
- Prior art keywords
- gene
- dna
- dna fragment
- polypeptide
- transformation products
- Prior art date
Links
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- 229940041514 candida albicans extract Drugs 0.000 description 1
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- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- IDLFZVILOHSSID-OVLDLUHVSA-N corticotropin Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=C(O)C=C1 IDLFZVILOHSSID-OVLDLUHVSA-N 0.000 description 1
- 229960000258 corticotropin Drugs 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 241001493065 dsRNA viruses Species 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
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- 239000000499 gel Substances 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 101150118316 ghoS gene Proteins 0.000 description 1
- 229960002989 glutamic acid Drugs 0.000 description 1
- 230000005484 gravity Effects 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 239000011874 heated mixture Substances 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 229960002773 hyaluronidase Drugs 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 229940116108 lactase Drugs 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229960004452 methionine Drugs 0.000 description 1
- 229960004857 mitomycin Drugs 0.000 description 1
- 239000002636 mycotoxin Substances 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229910052757 nitrogen Inorganic materials 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
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000003399 opiate peptide Substances 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 101150014208 pbg gene Proteins 0.000 description 1
- 101150049824 pstA gene Proteins 0.000 description 1
- 101150112050 pstB gene Proteins 0.000 description 1
- 101150013628 pstB1 gene Proteins 0.000 description 1
- 210000004196 psta Anatomy 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000001226 reprecipitation Methods 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000011120 smear test Methods 0.000 description 1
- 239000003998 snake venom Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000005507 spraying Methods 0.000 description 1
- 239000012192 staining solution Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- WPLOVIFNBMNBPD-ATHMIXSHSA-N subtilin Chemical compound CC1SCC(NC2=O)C(=O)NC(CC(N)=O)C(=O)NC(C(=O)NC(CCCCN)C(=O)NC(C(C)CC)C(=O)NC(=C)C(=O)NC(CCCCN)C(O)=O)CSC(C)C2NC(=O)C(CC(C)C)NC(=O)C1NC(=O)C(CCC(N)=O)NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C1NC(=O)C(=C/C)/NC(=O)C(CCC(N)=O)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)CNC(=O)C(NC(=O)C(NC(=O)C2NC(=O)CNC(=O)C3CCCN3C(=O)C(NC(=O)C3NC(=O)C(CC(C)C)NC(=O)C(=C)NC(=O)C(CCC(O)=O)NC(=O)C(NC(=O)C(CCCCN)NC(=O)C(N)CC=4C5=CC=CC=C5NC=4)CSC3)C(C)SC2)C(C)C)C(C)SC1)CC1=CC=CC=C1 WPLOVIFNBMNBPD-ATHMIXSHSA-N 0.000 description 1
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- 239000002699 waste material Substances 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- 101150069452 z gene Proteins 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2468—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1) acting on beta-galactose-glycoside bonds, e.g. carrageenases (3.2.1.83; 3.2.1.157); beta-agarase (3.2.1.81)
- C12N9/2471—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01023—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
- C07K2319/034—Fusion polypeptide containing a localisation/targetting motif containing a motif for targeting to the periplasmic space of Gram negative bacteria as a soluble protein, i.e. signal sequence should be cleaved
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/61—Fusion polypeptide containing an enzyme fusion for detection (lacZ, luciferase)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/822—Microorganisms using bacteria or actinomycetales
- Y10S435/848—Escherichia
- Y10S435/849—Escherichia coli
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP57096775A JPS592689A (ja) | 1982-06-04 | 1982-06-04 | 強力な遺伝子発現能を有する新規レプリコンの作成法 |
Publications (3)
Publication Number | Publication Date |
---|---|
SE8303068D0 SE8303068D0 (sv) | 1983-05-31 |
SE8303068L SE8303068L (sv) | 1983-12-05 |
SE459816B true SE459816B (sv) | 1989-08-07 |
Family
ID=14174007
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
SE8303068A SE459816B (sv) | 1982-06-04 | 1983-05-31 | Vektor med stark genexpression |
Country Status (9)
Families Citing this family (11)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPH0699580B2 (ja) * | 1986-05-28 | 1994-12-07 | 花王株式会社 | 多孔性フイルム |
FR2599380A1 (fr) * | 1986-05-29 | 1987-12-04 | Centre Nat Rech Scient | Vecteur d'exportation de proteines chez escherichiacoli, bacteries transformees et procede pour la preparation de proteines |
JPH0699581B2 (ja) * | 1986-06-09 | 1994-12-07 | 花王株式会社 | 多孔性フイルム |
JPH0768394B2 (ja) * | 1987-12-01 | 1995-07-26 | 花王株式会社 | 多孔性フィルム及びその製造方法 |
NZ228320A (en) | 1988-03-29 | 1991-06-25 | Du Pont | Nucleic acid promoter fragments of the promoter region homologous to the em gene of wheat, dna constructs therefrom and plants thereof |
US5139954A (en) * | 1988-03-29 | 1992-08-18 | E. I. Du Pont De Nemours And Company | DNA promoter fragments from wheat |
EP0388186A1 (en) * | 1989-03-17 | 1990-09-19 | E.I. Du Pont De Nemours And Company | External regulation of gene expression |
US5304472A (en) * | 1992-11-20 | 1994-04-19 | Genentech, Inc. | Method of controlling polypeptide production in bacterial cells |
US5965402A (en) * | 1996-02-20 | 1999-10-12 | Smithkline Beecham Corporation | DNA encoding phoH polypeptides |
WO1997035612A1 (fr) * | 1996-03-23 | 1997-10-02 | The Research Foundation For Microbial Diseases Of Osaka University | Antigene a fragment fonctionnel de la toxine du tetanos, et vaccin contre le tetanos |
DK3287523T3 (da) * | 2015-04-24 | 2022-07-25 | Ajinomoto Kk | Fremgangsmåde til sekretorisk fremstilling af protein |
Family Cites Families (9)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4237224A (en) * | 1974-11-04 | 1980-12-02 | Board Of Trustees Of The Leland Stanford Jr. University | Process for producing biologically functional molecular chimeras |
GB2023612B (en) * | 1978-06-01 | 1982-09-15 | Hopwood D A | Inc of nucleic acid into cellular systems streptomyces plasmids |
US4411994A (en) * | 1978-06-08 | 1983-10-25 | The President And Fellows Of Harvard College | Protein synthesis |
FR2441659A1 (fr) * | 1978-11-14 | 1980-06-13 | Anvar | Nouveaux plasmides hybrides et microorganismes les contenant |
US4273875A (en) * | 1979-03-05 | 1981-06-16 | The Upjohn Company | Plasmid and process of isolating same |
GB2052516B (en) * | 1979-06-01 | 1983-06-29 | Searle & Co | Plasmid vectors production and use thereof |
DE2931999A1 (de) * | 1979-08-03 | 1981-02-26 | Schering Ag | Herstellung und anwendung von neukombinierten plasmiden mit genen fuer alkalische phosphatasen |
NO159863C (no) * | 1980-01-07 | 1989-02-15 | Univ Rochester | Fremgangsm te for fremstilling og seleksjon av en rant bakteriofag som inneholder et genetisk fragment og koder for alfa-amylase, egnet for bruk i heterolog transformering av en bacillus-verts-mikroorganisme. |
US4374927A (en) * | 1981-02-24 | 1983-02-22 | The Board Of Trustees Of The Leland Stanford Jr. University | Extrachromosomal regulation of expression |
-
1982
- 1982-06-04 JP JP57096775A patent/JPS592689A/ja active Granted
-
1983
- 1983-05-25 CA CA000428884A patent/CA1202258A/en not_active Expired
- 1983-05-31 SE SE8303068A patent/SE459816B/sv not_active IP Right Cessation
- 1983-06-03 BE BE0/210930A patent/BE896957A/fr not_active IP Right Cessation
- 1983-06-03 NL NLAANVRAGE8301986,A patent/NL189208C/xx not_active IP Right Cessation
- 1983-06-03 FR FR8309292A patent/FR2528070B1/fr not_active Expired
- 1983-06-03 GB GB08315278A patent/GB2124232B/en not_active Expired
- 1983-06-04 DE DE19833320339 patent/DE3320339A1/de active Granted
- 1983-06-06 US US06/501,559 patent/US4703005A/en not_active Expired - Lifetime
Also Published As
Publication number | Publication date |
---|---|
US4703005A (en) | 1987-10-27 |
FR2528070B1 (fr) | 1987-07-31 |
GB2124232A (en) | 1984-02-15 |
NL189208C (nl) | 1993-02-01 |
DE3320339A1 (de) | 1984-01-19 |
JPS592689A (ja) | 1984-01-09 |
DE3320339C2 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1990-08-23 |
CA1202258A (en) | 1986-03-25 |
SE8303068D0 (sv) | 1983-05-31 |
BE896957A (fr) | 1983-12-05 |
GB2124232B (en) | 1985-12-18 |
FR2528070A1 (fr) | 1983-12-09 |
NL189208B (nl) | 1992-09-01 |
NL8301986A (nl) | 1984-01-02 |
GB8315278D0 (en) | 1983-07-06 |
SE8303068L (sv) | 1983-12-05 |
JPH0116159B2 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1989-03-23 |
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