AP730A - Gene expression in mammalian cells. - Google Patents

Gene expression in mammalian cells. Download PDF

Info

Publication number: AP730A
Authority: AP; ARIPO
Prior art keywords: cells; promoter; interferon; human; gene
Prior art date: 1995-03-24

Application number

APAP/P/1997/001091A

Other languages

English (en)

Other versions

AP9701091A0 (en

Inventor

Yin Hwee Tan

Wanjin Hong

Original Assignee

Inst Of Molecular And Cell Biology

Priority date (The priority date 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 date listed.)

1995-03-24

Filing date

1996-03-22

Publication date

1999-02-04

1996-03-22 Application filed by Inst Of Molecular And Cell Biology filed Critical Inst Of Molecular And Cell Biology

1997-10-31 Publication of AP9701091A0 publication Critical patent/AP9701091A0/xx

1999-02-04 Application granted granted Critical

1999-02-04 Publication of AP730A publication Critical patent/AP730A/en

Links

230000014509 gene expression Effects 0.000 title claims abstract description 71
210000004962 mammalian cell Anatomy 0.000 title claims abstract description 47
108090000623 proteins and genes Proteins 0.000 claims abstract description 73
108090000157 Metallothionein Proteins 0.000 claims abstract description 56
229910001385 heavy metal Inorganic materials 0.000 claims abstract description 46
150000002500 ions Chemical class 0.000 claims abstract description 41
108091026890 Coding region Proteins 0.000 claims abstract description 34
102000004169 proteins and genes Human genes 0.000 claims abstract description 34
241001045988 Neogene Species 0.000 claims abstract description 33
239000003550 marker Substances 0.000 claims abstract description 33
101150091879 neo gene Proteins 0.000 claims abstract description 33
101000987586 Homo sapiens Eosinophil peroxidase Proteins 0.000 claims abstract description 14
101000920686 Homo sapiens Erythropoietin Proteins 0.000 claims abstract description 14
102000044890 human EPO Human genes 0.000 claims abstract description 13
150000007523 nucleic acids Chemical group 0.000 claims abstract description 10
108091028043 Nucleic acid sequence Proteins 0.000 claims abstract description 6
238000012258 culturing Methods 0.000 claims abstract description 4
210000004027 cell Anatomy 0.000 claims description 138
239000013598 vector Substances 0.000 claims description 73
229940079322 interferon Drugs 0.000 claims description 59
108090000467 Interferon-beta Proteins 0.000 claims description 49
102000003996 Interferon-beta Human genes 0.000 claims description 42
238000000034 method Methods 0.000 claims description 39
102000014150 Interferons Human genes 0.000 claims description 29
108010050904 Interferons Proteins 0.000 claims description 29
239000003623 enhancer Substances 0.000 claims description 25
241000283973 Oryctolagus cuniculus Species 0.000 claims description 24
210000004978 chinese hamster ovary cell Anatomy 0.000 claims description 19
239000013612 plasmid Substances 0.000 claims description 19
210000002966 serum Anatomy 0.000 claims description 18
230000000694 effects Effects 0.000 claims description 17
BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Chemical compound O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 claims description 16
230000001965 increasing effect Effects 0.000 claims description 15
241000700605 Viruses Species 0.000 claims description 9
108020004414 DNA Proteins 0.000 claims description 8
206010039491 Sarcoma Diseases 0.000 claims description 8
108091003079 Bovine Serum Albumin Proteins 0.000 claims description 7
238000002360 preparation method Methods 0.000 claims description 5
108020004707 nucleic acids Proteins 0.000 claims description 4
102000039446 nucleic acids Human genes 0.000 claims description 4
239000003085 diluting agent Substances 0.000 claims description 3
239000003937 drug carrier Substances 0.000 claims description 3
239000008194 pharmaceutical composition Substances 0.000 claims description 3
229920001542 oligosaccharide Polymers 0.000 description 35
150000002482 oligosaccharides Chemical class 0.000 description 35
210000002950 fibroblast Anatomy 0.000 description 17
PXBFMLJZNCDSMP-UHFFFAOYSA-N 2-Aminobenzamide Chemical compound NC(=O)C1=CC=CC=C1N PXBFMLJZNCDSMP-UHFFFAOYSA-N 0.000 description 15
241000588724 Escherichia coli Species 0.000 description 15
101150074155 DHFR gene Proteins 0.000 description 14
102100040019 Interferon alpha-1/13 Human genes 0.000 description 14
239000012634 fragment Substances 0.000 description 13
239000011734 sodium Substances 0.000 description 13
102000003951 Erythropoietin Human genes 0.000 description 12
108090000394 Erythropoietin Proteins 0.000 description 12
230000000840 anti-viral effect Effects 0.000 description 12
229940105423 erythropoietin Drugs 0.000 description 12
OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 12
239000002609 medium Substances 0.000 description 11
108010005714 Interferon beta-1b Proteins 0.000 description 10
230000002378 acidificating effect Effects 0.000 description 10
229940021459 betaseron Drugs 0.000 description 10
230000003612 virological effect Effects 0.000 description 10
DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 9
102000003792 Metallothionein Human genes 0.000 description 9
239000013604 expression vector Substances 0.000 description 9
230000010076 replication Effects 0.000 description 9
241000701022 Cytomegalovirus Species 0.000 description 8
102000016622 Dipeptidyl Peptidase 4 Human genes 0.000 description 8
101000930822 Giardia intestinalis Dipeptidyl-peptidase 4 Proteins 0.000 description 8
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 8
239000012679 serum free medium Substances 0.000 description 7
RJURFGZVJUQBHK-UHFFFAOYSA-N actinomycin D Natural products CC1OC(=O)C(C(C)C)N(C)C(=O)CN(C)C(=O)C2CCCN2C(=O)C(C(C)C)NC(=O)C1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)NC4C(=O)NC(C(N5CCCC5C(=O)N(C)CC(=O)N(C)C(C(C)C)C(=O)OC4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-UHFFFAOYSA-N 0.000 description 6
210000004369 blood Anatomy 0.000 description 6
239000008280 blood Substances 0.000 description 6
229910052793 cadmium Inorganic materials 0.000 description 6
BDOSMKKIYDKNTQ-UHFFFAOYSA-N cadmium atom Chemical compound [Cd] BDOSMKKIYDKNTQ-UHFFFAOYSA-N 0.000 description 6
238000004519 manufacturing process Methods 0.000 description 6
239000000047 product Substances 0.000 description 6
238000001262 western blot Methods 0.000 description 6
206010028980 Neoplasm Diseases 0.000 description 5
241000714474 Rous sarcoma virus Species 0.000 description 5
238000004458 analytical method Methods 0.000 description 5
230000001580 bacterial effect Effects 0.000 description 5
238000009826 distribution Methods 0.000 description 5
229940047124 interferons Drugs 0.000 description 5
229960000485 methotrexate Drugs 0.000 description 5
230000007935 neutral effect Effects 0.000 description 5
238000011282 treatment Methods 0.000 description 5
FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 4
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
239000002299 complementary DNA Substances 0.000 description 4
239000001963 growth medium Substances 0.000 description 4
238000003306 harvesting Methods 0.000 description 4
238000003119 immunoblot Methods 0.000 description 4
239000000203 mixture Substances 0.000 description 4
230000008488 polyadenylation Effects 0.000 description 4
238000011084 recovery Methods 0.000 description 4
UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
125000001424 substituent group Chemical group 0.000 description 4
231100000331 toxic Toxicity 0.000 description 4
230000002588 toxic effect Effects 0.000 description 4
238000011144 upstream manufacturing Methods 0.000 description 4
239000011701 zinc Substances 0.000 description 4
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
-1 Cd2' Chemical class 0.000 description 3
108010092160 Dactinomycin Proteins 0.000 description 3
229920002307 Dextran Polymers 0.000 description 3
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 3
LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 3
240000007711 Peperomia pellucida Species 0.000 description 3
RJURFGZVJUQBHK-IIXSONLDSA-N actinomycin D Chemical compound C[C@H]1OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]2CCCN2C(=O)[C@@H](C(C)C)NC(=O)[C@H]1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)N[C@@H]4C(=O)N[C@@H](C(N5CCC[C@H]5C(=O)N(C)CC(=O)N(C)[C@@H](C(C)C)C(=O)O[C@@H]4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-IIXSONLDSA-N 0.000 description 3
229960000723 ampicillin Drugs 0.000 description 3
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 3
230000003115 biocidal effect Effects 0.000 description 3
230000004071 biological effect Effects 0.000 description 3
150000001720 carbohydrates Chemical group 0.000 description 3
239000010949 copper Substances 0.000 description 3
229960000640 dactinomycin Drugs 0.000 description 3
238000001514 detection method Methods 0.000 description 3
201000010099 disease Diseases 0.000 description 3
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
239000000499 gel Substances 0.000 description 3
239000008103 glucose Substances 0.000 description 3
208000006359 hepatoblastoma Diseases 0.000 description 3
238000003780 insertion Methods 0.000 description 3
230000037431 insertion Effects 0.000 description 3
230000010354 integration Effects 0.000 description 3
229930027917 kanamycin Natural products 0.000 description 3
229960000318 kanamycin Drugs 0.000 description 3
SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 3
229930182823 kanamycin A Natural products 0.000 description 3
239000002773 nucleotide Substances 0.000 description 3
125000003729 nucleotide group Chemical group 0.000 description 3
239000013600 plasmid vector Substances 0.000 description 3
108091008146 restriction endonucleases Proteins 0.000 description 3
230000010473 stable expression Effects 0.000 description 3
238000010254 subcutaneous injection Methods 0.000 description 3
239000007929 subcutaneous injection Substances 0.000 description 3
238000002560 therapeutic procedure Methods 0.000 description 3
239000003656 tris buffered saline Substances 0.000 description 3
CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
102000011022 Chorionic Gonadotropin Human genes 0.000 description 2
108010062540 Chorionic Gonadotropin Proteins 0.000 description 2
108020004705 Codon Proteins 0.000 description 2
208000035473 Communicable disease Diseases 0.000 description 2
108010017826 DNA Polymerase I Proteins 0.000 description 2
102000004594 DNA Polymerase I Human genes 0.000 description 2
102000004190 Enzymes Human genes 0.000 description 2
108090000790 Enzymes Proteins 0.000 description 2
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
102000003886 Glycoproteins Human genes 0.000 description 2
108090000288 Glycoproteins Proteins 0.000 description 2
108091006905 Human Serum Albumin Proteins 0.000 description 2
102000008100 Human Serum Albumin Human genes 0.000 description 2
OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 2
206010020751 Hypersensitivity Diseases 0.000 description 2
102000005348 Neuraminidase Human genes 0.000 description 2
108010006232 Neuraminidase Proteins 0.000 description 2
108010067390 Viral Proteins Proteins 0.000 description 2
208000036142 Viral infection Diseases 0.000 description 2
238000000246 agarose gel electrophoresis Methods 0.000 description 2
208000026935 allergic disease Diseases 0.000 description 2
230000007815 allergy Effects 0.000 description 2
APKFDSVGJQXUKY-INPOYWNPSA-N amphotericin B Chemical compound O[C@H]1[C@@H](N)[C@H](O)[C@@H](C)O[C@H]1O[C@H]1/C=C/C=C/C=C/C=C/C=C/C=C/C=C/[C@H](C)[C@@H](O)[C@@H](C)[C@H](C)OC(=O)C[C@H](O)C[C@H](O)CC[C@@H](O)[C@H](O)C[C@H](O)C[C@](O)(C[C@H](O)[C@H]2C(O)=O)O[C@H]2C1 APKFDSVGJQXUKY-INPOYWNPSA-N 0.000 description 2
238000005349 anion exchange Methods 0.000 description 2
238000005571 anion exchange chromatography Methods 0.000 description 2
238000003556 assay Methods 0.000 description 2
229940098773 bovine serum albumin Drugs 0.000 description 2
235000014633 carbohydrates Nutrition 0.000 description 2
230000010261 cell growth Effects 0.000 description 2
150000001793 charged compounds Chemical class 0.000 description 2
238000004587 chromatography analysis Methods 0.000 description 2
238000004440 column chromatography Methods 0.000 description 2
229940079593 drug Drugs 0.000 description 2
239000003814 drug Substances 0.000 description 2
239000003480 eluent Substances 0.000 description 2
230000002708 enhancing effect Effects 0.000 description 2
239000000284 extract Substances 0.000 description 2
239000012894 fetal calf serum Substances 0.000 description 2
239000012530 fluid Substances 0.000 description 2
210000003953 foreskin Anatomy 0.000 description 2
238000009472 formulation Methods 0.000 description 2
238000005227 gel permeation chromatography Methods 0.000 description 2
125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 2
230000013595 glycosylation Effects 0.000 description 2
238000006206 glycosylation reaction Methods 0.000 description 2
239000003102 growth factor Substances 0.000 description 2
229940084986 human chorionic gonadotropin Drugs 0.000 description 2
239000000411 inducer Substances 0.000 description 2
208000015181 infectious disease Diseases 0.000 description 2
230000000977 initiatory effect Effects 0.000 description 2
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
238000001990 intravenous administration Methods 0.000 description 2
239000000463 material Substances 0.000 description 2
239000011159 matrix material Substances 0.000 description 2
238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 2
108020004999 messenger RNA Proteins 0.000 description 2
230000004048 modification Effects 0.000 description 2
238000012986 modification Methods 0.000 description 2
238000010369 molecular cloning Methods 0.000 description 2
230000036961 partial effect Effects 0.000 description 2
239000002245 particle Substances 0.000 description 2
YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
229920003023 plastic Polymers 0.000 description 2
238000000746 purification Methods 0.000 description 2
238000010187 selection method Methods 0.000 description 2
238000012163 sequencing technique Methods 0.000 description 2
239000011780 sodium chloride Substances 0.000 description 2
229960005322 streptomycin Drugs 0.000 description 2
210000003462 vein Anatomy 0.000 description 2
230000009385 viral infection Effects 0.000 description 2
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
210000005253 yeast cell Anatomy 0.000 description 2
HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
KZDCMKVLEYCGQX-UDPGNSCCSA-N 2-(diethylamino)ethyl 4-aminobenzoate;(2s,5r,6r)-3,3-dimethyl-7-oxo-6-[(2-phenylacetyl)amino]-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid;hydrate Chemical compound O.CCN(CC)CCOC(=O)C1=CC=C(N)C=C1.N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 KZDCMKVLEYCGQX-UDPGNSCCSA-N 0.000 description 1
101150090724 3 gene Proteins 0.000 description 1
SHZGCJCMOBCMKK-UHFFFAOYSA-N 6-methyloxane-2,3,4,5-tetrol Chemical compound CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 1
208000030507 AIDS Diseases 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
229930183010 Amphotericin Natural products 0.000 description 1
QGGFZZLFKABGNL-UHFFFAOYSA-N Amphotericin A Natural products OC1C(N)C(O)C(C)OC1OC1C=CC=CC=CC=CCCC=CC=CC(C)C(O)C(C)C(C)OC(=O)CC(O)CC(O)CCC(O)C(O)CC(O)CC(O)(CC(O)C2C(O)=O)OC2C1 QGGFZZLFKABGNL-UHFFFAOYSA-N 0.000 description 1
APKFDSVGJQXUKY-KKGHZKTASA-N Amphotericin-B Natural products O[C@H]1[C@@H](N)[C@H](O)[C@@H](C)O[C@H]1O[C@H]1C=CC=CC=CC=CC=CC=CC=C[C@H](C)[C@@H](O)[C@@H](C)[C@H](C)OC(=O)C[C@H](O)C[C@H](O)CC[C@@H](O)[C@H](O)C[C@H](O)C[C@](O)(C[C@H](O)[C@H]2C(O)=O)O[C@H]2C1 APKFDSVGJQXUKY-KKGHZKTASA-N 0.000 description 1
241000186063 Arthrobacter Species 0.000 description 1
BHELIUBJHYAEDK-OAIUPTLZSA-N Aspoxicillin Chemical compound C1([C@H](C(=O)N[C@@H]2C(N3[C@H](C(C)(C)S[C@@H]32)C(O)=O)=O)NC(=O)[C@H](N)CC(=O)NC)=CC=C(O)C=C1 BHELIUBJHYAEDK-OAIUPTLZSA-N 0.000 description 1
208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 description 1
241000894006 Bacteria Species 0.000 description 1
208000003174 Brain Neoplasms Diseases 0.000 description 1
208000014644 Brain disease Diseases 0.000 description 1
206010008263 Cervical dysplasia Diseases 0.000 description 1
VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
208000010833 Chronic myeloid leukaemia Diseases 0.000 description 1
RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
241000699802 Cricetulus griseus Species 0.000 description 1
JPVYNHNXODAKFH-UHFFFAOYSA-N Cu2+ Chemical compound [Cu+2] JPVYNHNXODAKFH-UHFFFAOYSA-N 0.000 description 1
102000004127 Cytokines Human genes 0.000 description 1
108090000695 Cytokines Proteins 0.000 description 1
208000001490 Dengue Diseases 0.000 description 1
206010012310 Dengue fever Diseases 0.000 description 1
206010014612 Encephalitis viral Diseases 0.000 description 1
208000005176 Hepatitis C Diseases 0.000 description 1
241000238631 Hexapoda Species 0.000 description 1
241000282412 Homo Species 0.000 description 1
102000002265 Human Growth Hormone Human genes 0.000 description 1
108010000521 Human Growth Hormone Proteins 0.000 description 1
239000000854 Human Growth Hormone Substances 0.000 description 1
101150103227 IFN gene Proteins 0.000 description 1
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
102100023915 Insulin Human genes 0.000 description 1
108090001061 Insulin Proteins 0.000 description 1
102000013462 Interleukin-12 Human genes 0.000 description 1
108010065805 Interleukin-12 Proteins 0.000 description 1
102000015696 Interleukins Human genes 0.000 description 1
108010063738 Interleukins Proteins 0.000 description 1
102100024319 Intestinal-type alkaline phosphatase Human genes 0.000 description 1
101710184243 Intestinal-type alkaline phosphatase Proteins 0.000 description 1
108091092195 Intron Proteins 0.000 description 1
PNIWLNAGKUGXDO-UHFFFAOYSA-N Lactosamine Natural products OC1C(N)C(O)OC(CO)C1OC1C(O)C(O)C(O)C(CO)O1 PNIWLNAGKUGXDO-UHFFFAOYSA-N 0.000 description 1
206010058467 Lung neoplasm malignant Diseases 0.000 description 1
241000713333 Mouse mammary tumor virus Species 0.000 description 1
241000204031 Mycoplasma Species 0.000 description 1
OVRNDRQMDRJTHS-BKJPEWSUSA-N N-acetyl-D-hexosamine Chemical compound CC(=O)NC1C(O)O[C@H](CO)C(O)C1O OVRNDRQMDRJTHS-BKJPEWSUSA-N 0.000 description 1
OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acetylhexosamine Chemical compound CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 1
208000002454 Nasopharyngeal Carcinoma Diseases 0.000 description 1
206010061306 Nasopharyngeal cancer Diseases 0.000 description 1
239000000020 Nitrocellulose Substances 0.000 description 1
108091034117 Oligonucleotide Proteins 0.000 description 1
108700026244 Open Reading Frames Proteins 0.000 description 1
229930182555 Penicillin Natural products 0.000 description 1
JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
108010077524 Peptide Elongation Factor 1 Proteins 0.000 description 1
108010002747 Pfu DNA polymerase Proteins 0.000 description 1
101100229216 Pisum sativum GS3B gene Proteins 0.000 description 1
206010035737 Pneumonia viral Diseases 0.000 description 1
208000006265 Renal cell carcinoma Diseases 0.000 description 1
101710126382 Signal recognition particle receptor subunit alpha Proteins 0.000 description 1
102100026900 Signal recognition particle receptor subunit alpha Human genes 0.000 description 1
101710111458 Signal recognition particle receptor subunit alpha homolog Proteins 0.000 description 1
FKNQFGJONOIPTF-UHFFFAOYSA-N Sodium cation Chemical compound [Na+] FKNQFGJONOIPTF-UHFFFAOYSA-N 0.000 description 1
108091081024 Start codon Proteins 0.000 description 1
QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
108010022394 Threonine synthase Proteins 0.000 description 1
102100037116 Transcription elongation factor 1 homolog Human genes 0.000 description 1
102000004338 Transferrin Human genes 0.000 description 1
108090000901 Transferrin Proteins 0.000 description 1
HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
239000007983 Tris buffer Substances 0.000 description 1
229920004890 Triton X-100 Polymers 0.000 description 1
239000013504 Triton X-100 Substances 0.000 description 1
HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
PTFCDOFLOPIGGS-UHFFFAOYSA-N Zinc dication Chemical compound [Zn+2] PTFCDOFLOPIGGS-UHFFFAOYSA-N 0.000 description 1
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
239000002253 acid Substances 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
150000001413 amino acids Chemical class 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
229940009444 amphotericin Drugs 0.000 description 1
229960003942 amphotericin b Drugs 0.000 description 1
230000003321 amplification Effects 0.000 description 1
208000000252 angiomatosis Diseases 0.000 description 1
239000003242 anti bacterial agent Substances 0.000 description 1
229940088710 antibiotic agent Drugs 0.000 description 1
239000000427 antigen Substances 0.000 description 1
102000036639 antigens Human genes 0.000 description 1
108091007433 antigens Proteins 0.000 description 1
239000002246 antineoplastic agent Substances 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
210000001367 artery Anatomy 0.000 description 1
230000001174 ascending effect Effects 0.000 description 1
239000003855 balanced salt solution Substances 0.000 description 1
230000009286 beneficial effect Effects 0.000 description 1
230000037396 body weight Effects 0.000 description 1
WLZRMCYVCSSEQC-UHFFFAOYSA-N cadmium(2+) Chemical compound [Cd+2] WLZRMCYVCSSEQC-UHFFFAOYSA-N 0.000 description 1
239000001506 calcium phosphate Substances 0.000 description 1
229910000389 calcium phosphate Inorganic materials 0.000 description 1
235000011010 calcium phosphates Nutrition 0.000 description 1
244000309466 calf Species 0.000 description 1
201000011510 cancer Diseases 0.000 description 1
239000002775 capsule Substances 0.000 description 1
239000001569 carbon dioxide Substances 0.000 description 1
229910002092 carbon dioxide Inorganic materials 0.000 description 1
238000000006 cell growth inhibition assay Methods 0.000 description 1
210000000170 cell membrane Anatomy 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
208000007951 cervical intraepithelial neoplasia Diseases 0.000 description 1
239000012627 chemopreventive agent Substances 0.000 description 1
229940124443 chemopreventive agent Drugs 0.000 description 1
230000000973 chemotherapeutic effect Effects 0.000 description 1
230000002759 chromosomal effect Effects 0.000 description 1
238000010367 cloning Methods 0.000 description 1
230000021615 conjugation Effects 0.000 description 1
238000010276 construction Methods 0.000 description 1
238000011109 contamination Methods 0.000 description 1
229910052802 copper Inorganic materials 0.000 description 1
229910001431 copper ion Inorganic materials 0.000 description 1
238000005520 cutting process Methods 0.000 description 1
230000016396 cytokine production Effects 0.000 description 1
238000001804 debridement Methods 0.000 description 1
230000007423 decrease Effects 0.000 description 1
230000002950 deficient Effects 0.000 description 1
208000025729 dengue disease Diseases 0.000 description 1
238000003795 desorption Methods 0.000 description 1
238000011161 development Methods 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
239000002552 dosage form Substances 0.000 description 1
238000004520 electroporation Methods 0.000 description 1
238000010828 elution Methods 0.000 description 1
238000001976 enzyme digestion Methods 0.000 description 1
210000003527 eukaryotic cell Anatomy 0.000 description 1
230000001747 exhibiting effect Effects 0.000 description 1
108010056732 factor EF-P Proteins 0.000 description 1
238000004108 freeze drying Methods 0.000 description 1
230000004927 fusion Effects 0.000 description 1
238000010353 genetic engineering Methods 0.000 description 1
150000004676 glycans Chemical class 0.000 description 1
230000012010 growth Effects 0.000 description 1
208000002672 hepatitis B Diseases 0.000 description 1
150000002402 hexoses Chemical class 0.000 description 1
210000005260 human cell Anatomy 0.000 description 1
239000000413 hydrolysate Substances 0.000 description 1
238000000099 in vitro assay Methods 0.000 description 1
238000001727 in vivo Methods 0.000 description 1
238000011534 incubation Methods 0.000 description 1
230000001939 inductive effect Effects 0.000 description 1
230000002458 infectious effect Effects 0.000 description 1
239000004615 ingredient Substances 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
229940117681 interleukin-12 Drugs 0.000 description 1
229940047122 interleukins Drugs 0.000 description 1
230000003834 intracellular effect Effects 0.000 description 1
238000010255 intramuscular injection Methods 0.000 description 1
239000007927 intramuscular injection Substances 0.000 description 1
238000005342 ion exchange Methods 0.000 description 1
206010023332 keratitis Diseases 0.000 description 1
210000003734 kidney Anatomy 0.000 description 1
DOVBXGDYENZJBJ-ONMPCKGSSA-N lactosamine Chemical compound O=C[C@H](N)[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O DOVBXGDYENZJBJ-ONMPCKGSSA-N 0.000 description 1
239000007788 liquid Substances 0.000 description 1
239000006193 liquid solution Substances 0.000 description 1
239000006194 liquid suspension Substances 0.000 description 1
201000005202 lung cancer Diseases 0.000 description 1
208000020816 lung neoplasm Diseases 0.000 description 1
238000013507 mapping Methods 0.000 description 1
238000004949 mass spectrometry Methods 0.000 description 1
238000001819 mass spectrum Methods 0.000 description 1
238000001254 matrix assisted laser desorption--ionisation time-of-flight mass spectrum Methods 0.000 description 1
238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 1
238000005259 measurement Methods 0.000 description 1
230000001404 mediated effect Effects 0.000 description 1
201000001441 melanoma Diseases 0.000 description 1
239000012528 membrane Substances 0.000 description 1
239000012569 microbial contaminant Substances 0.000 description 1
230000000813 microbial effect Effects 0.000 description 1
201000006417 multiple sclerosis Diseases 0.000 description 1
201000011216 nasopharynx carcinoma Diseases 0.000 description 1
229920001220 nitrocellulos Polymers 0.000 description 1
238000010899 nucleation Methods 0.000 description 1
238000003199 nucleic acid amplification method Methods 0.000 description 1
230000000771 oncological effect Effects 0.000 description 1
210000001672 ovary Anatomy 0.000 description 1
238000004816 paper chromatography Methods 0.000 description 1
229940049954 penicillin Drugs 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
239000002504 physiological saline solution Substances 0.000 description 1
230000001124 posttranscriptional effect Effects 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
230000037452 priming Effects 0.000 description 1
210000001236 prokaryotic cell Anatomy 0.000 description 1
230000000644 propagated effect Effects 0.000 description 1
238000006268 reductive amination reaction Methods 0.000 description 1
230000001105 regulatory effect Effects 0.000 description 1
230000001177 retroviral effect Effects 0.000 description 1
230000002441 reversible effect Effects 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
230000003248 secreting effect Effects 0.000 description 1
230000028327 secretion Effects 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
125000005629 sialic acid group Chemical group 0.000 description 1
230000009450 sialylation Effects 0.000 description 1
201000010153 skin papilloma Diseases 0.000 description 1
229910052708 sodium Inorganic materials 0.000 description 1
229910001415 sodium ion Inorganic materials 0.000 description 1
239000007787 solid Substances 0.000 description 1
239000000243 solution Substances 0.000 description 1
241000894007 species Species 0.000 description 1
239000000126 substance Substances 0.000 description 1
229910021653 sulphate ion Inorganic materials 0.000 description 1
239000013589 supplement Substances 0.000 description 1
239000003826 tablet Substances 0.000 description 1
238000012360 testing method Methods 0.000 description 1
231100000419 toxicity Toxicity 0.000 description 1
230000001988 toxicity Effects 0.000 description 1
238000013518 transcription Methods 0.000 description 1
230000035897 transcription Effects 0.000 description 1
230000002103 transcriptional effect Effects 0.000 description 1
238000001890 transfection Methods 0.000 description 1
239000012581 transferrin Substances 0.000 description 1
238000013519 translation Methods 0.000 description 1
230000014621 translational initiation Effects 0.000 description 1
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
VSQQQLOSPVPRAZ-RRKCRQDMSA-N trifluridine Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(C(F)(F)F)=C1 VSQQQLOSPVPRAZ-RRKCRQDMSA-N 0.000 description 1
229960003962 trifluridine Drugs 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
210000004881 tumor cell Anatomy 0.000 description 1
241001529453 unidentified herpesvirus Species 0.000 description 1
229960005486 vaccine Drugs 0.000 description 1
239000003981 vehicle Substances 0.000 description 1
201000002498 viral encephalitis Diseases 0.000 description 1
208000009421 viral pneumonia Diseases 0.000 description 1
239000011800 void material Substances 0.000 description 1
229910052725 zinc Inorganic materials 0.000 description 1
NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
235000009529 zinc sulphate Nutrition 0.000 description 1
239000011686 zinc sulphate Substances 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
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/565—IFN-beta
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/18—Growth factors; Growth regulators
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/505—Erythropoietin [EPO]
- 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
- 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
- C12N15/85—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- 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
- C12N2800/00—Nucleic acids vectors
- C12N2800/10—Plasmid DNA
- C12N2800/108—Plasmid DNA episomal vectors
- 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
- C12N2830/00—Vector systems having a special element relevant for transcription
- C12N2830/001—Vector systems having a special element relevant for transcription controllable enhancer/promoter combination
- C12N2830/002—Vector systems having a special element relevant for transcription controllable enhancer/promoter combination inducible enhancer/promoter combination, e.g. hypoxia, iron, transcription factor
- 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
- C12N2830/00—Vector systems having a special element relevant for transcription
- C12N2830/15—Vector systems having a special element relevant for transcription chimeric enhancer/promoter combination
- 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
- C12N2830/00—Vector systems having a special element relevant for transcription
- C12N2830/60—Vector systems having a special element relevant for transcription from viruses
- 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
- C12N2830/00—Vector systems having a special element relevant for transcription
- C12N2830/80—Vector systems having a special element relevant for transcription from vertebrates
- C12N2830/85—Vector systems having a special element relevant for transcription from vertebrates mammalian

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Genetics & Genomics (AREA)
Organic Chemistry (AREA)
Zoology (AREA)
Engineering & Computer Science (AREA)
General Health & Medical Sciences (AREA)
Molecular Biology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
Bioinformatics & Cheminformatics (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
General Engineering & Computer Science (AREA)
Wood Science & Technology (AREA)
Medicinal Chemistry (AREA)
Gastroenterology & Hepatology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Toxicology (AREA)
Microbiology (AREA)
Plant Pathology (AREA)
Physics & Mathematics (AREA)
Public Health (AREA)
Animal Behavior & Ethology (AREA)
Pharmacology & Pharmacy (AREA)
Veterinary Medicine (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Chemical Kinetics & Catalysis (AREA)
Virology (AREA)
Oncology (AREA)
General Chemical & Material Sciences (AREA)
Communicable Diseases (AREA)
Immunology (AREA)
Epidemiology (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

APAP/P/1997/001091A 1995-03-24 1996-03-22 Gene expression in mammalian cells. AP730A (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
GBGB9506051.3A GB9506051D0 (en)	1995-03-24	1995-03-24	Gene expression
PCT/CA1996/000174 WO1996030531A1 (en)	1995-03-24	1996-03-22	Gene expression in mammalian cells

Publications (2)

Publication Number	Publication Date
AP9701091A0 AP9701091A0 (en)	1997-10-31
AP730A true AP730A (en)	1999-02-04

Family

ID=10771834

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
APAP/P/1997/001091A AP730A (en)	1995-03-24	1996-03-22	Gene expression in mammalian cells.

Country Status (15)

Country	Link
US (1)	US6207146B1 (no)
EP (1)	EP0815251A1 (no)
JP (1)	JPH11502705A (no)
KR (1)	KR19980703275A (no)
CN (1)	CN1185180A (no)
AP (1)	AP730A (no)
AU (1)	AU722341B2 (no)
BR (1)	BR9607831A (no)
CA (1)	CA2216174A1 (no)
GB (2)	GB9506051D0 (no)
HU (1)	HUP9800520A3 (no)
IL (1)	IL117594A (no)
NO (1)	NO974367L (no)
NZ (1)	NZ303133A (no)
WO (1)	WO1996030531A1 (no)

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
AU2002310922A1 (en) *	2001-05-04	2002-11-18	Institute Of Molecular And Cell Biology	Interferons in the treatment of ischemia
FR2843973B1 (fr) *	2002-08-30	2006-07-07	Agronomique Inst Nat Rech	Cassettes d'expression procaryotes regulees par le zinc
GB0524782D0 (en) *	2005-12-05	2006-01-11	Chiron Srl	Analysis of samples
CN100432230C (zh) *	2006-05-11	2008-11-12	南京大学	一种金属硫蛋白融合表达方法及其应用
EP2205752B1 (en) *	2007-10-25	2016-08-10	Sangamo BioSciences, Inc.	Methods and compositions for targeted integration
DK3768846T5 (da) *	2018-03-21	2024-08-19	Aldevron L L C	Virale og ikke-virale nanoplasmidvektorer med forbedret produktion

Citations (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0270799A1 (en) *	1986-10-27	1988-06-15	Cetus Oncology Corporation	Pharmaceutical compositions of recombinant beta-interferon and formulation processes
EP0529300A1 (de) *	1991-08-27	1993-03-03	Dr. Rentschler Biotechnologie GmbH	Neues rekombinantes Human-IFN-beta, Verfahren zu dessen Herstellung und dieses enthaltende pharmazeutische Zubereitungen
EP0551535A1 (en) *	1992-01-13	1993-07-21	SCLAVO S.p.A.	Process for the purification of recombinant human beta interferon, beta interferon thus purified, and pharmaceutical compositions which contain them

Family Cites Families (8)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5514567A (en)	1979-01-30	1996-05-07	Juridical Foundation, Japanese Foundation For Cancer Research	DNA and recombinant plasmid
AU538665B2 (en)	1979-10-30	1984-08-23	Juridical Foundation, Japanese Foundation For Cancer Research	Human interferon dna
US4966843A (en)	1982-11-01	1990-10-30	Cetus Corporation	Expression of interferon genes in Chinese hamster ovary cells
AU580145B2 (en) *	1985-02-13	1989-01-05	Scios Nova Inc.	Human metallothionein-ii promoter in mammalian expression system
GB2177914B (en)	1985-06-04	1989-10-25	Chugai Pharmaceutical Co Ltd	A pharmaceutical composition containing human erythropoietin and a surface active agent for nasal administration for the treatment of anemia
US4954437A (en) *	1986-09-15	1990-09-04	Integrated Genetics, Inc.	Cell encoding recombinant human erythropoietin
DE3712564A1 (de)	1987-04-14	1988-11-24	Bioferon Biochem Substanz	Verfahren zur konstruktion einer animalen zellinie fuer die herstellung von humanem interferon-beta
DD287531A5 (de) *	1988-06-16	1991-02-28	Akademie Der Wissenschaften,De	Verfahren zur herstellung von humanem wachstumshormon (sth) in tierischen zellen

1995
- 1995-03-24 GB GBGB9506051.3A patent/GB9506051D0/en active Pending
1996
- 1996-03-21 IL IL11759496A patent/IL117594A/en not_active IP Right Cessation
- 1996-03-22 EP EP96905646A patent/EP0815251A1/en not_active Withdrawn
- 1996-03-22 NZ NZ303133A patent/NZ303133A/xx unknown
- 1996-03-22 AU AU49358/96A patent/AU722341B2/en not_active Ceased
- 1996-03-22 CN CN96194053A patent/CN1185180A/zh active Pending
- 1996-03-22 US US08/913,778 patent/US6207146B1/en not_active Expired - Fee Related
- 1996-03-22 CA CA002216174A patent/CA2216174A1/en not_active Abandoned
- 1996-03-22 WO PCT/CA1996/000174 patent/WO1996030531A1/en not_active Ceased
- 1996-03-22 HU HU9800520A patent/HUP9800520A3/hu unknown
- 1996-03-22 BR BR9607831-6A patent/BR9607831A/pt not_active Application Discontinuation
- 1996-03-22 AP APAP/P/1997/001091A patent/AP730A/en active
- 1996-03-22 JP JP8528730A patent/JPH11502705A/ja not_active Withdrawn
- 1996-03-22 GB GB9720467A patent/GB2314332B/en not_active Expired - Fee Related
- 1996-03-22 KR KR1019970706679A patent/KR19980703275A/ko not_active Ceased
1997
- 1997-09-22 NO NO974367A patent/NO974367L/no not_active Application Discontinuation

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0270799A1 (en) *	1986-10-27	1988-06-15	Cetus Oncology Corporation	Pharmaceutical compositions of recombinant beta-interferon and formulation processes
EP0529300A1 (de) *	1991-08-27	1993-03-03	Dr. Rentschler Biotechnologie GmbH	Neues rekombinantes Human-IFN-beta, Verfahren zu dessen Herstellung und dieses enthaltende pharmazeutische Zubereitungen
EP0551535A1 (en) *	1992-01-13	1993-07-21	SCLAVO S.p.A.	Process for the purification of recombinant human beta interferon, beta interferon thus purified, and pharmaceutical compositions which contain them

Also Published As

Publication number	Publication date
BR9607831A (pt)	1999-11-30
MX9707244A (es)	1998-08-30
KR19980703275A (ko)	1998-10-15
NO974367L (no)	1997-11-24
HUP9800520A2 (hu)	1998-06-29
WO1996030531A1 (en)	1996-10-03
IL117594A (en)	2002-11-10
CA2216174A1 (en)	1996-10-03
AP9701091A0 (en)	1997-10-31
GB9720467D0 (en)	1997-11-26
EP0815251A1 (en)	1998-01-07
HK1005248A1 (en)	1998-12-31
GB9506051D0 (en)	1995-05-10
IL117594A0 (en)	1996-07-23
AU4935896A (en)	1996-10-16
GB2314332A (en)	1997-12-24
JPH11502705A (ja)	1999-03-09
AU722341B2 (en)	2000-07-27
GB2314332B (en)	1999-06-30
US6207146B1 (en)	2001-03-27
NO974367D0 (no)	1997-09-22
NZ303133A (en)	1999-11-29
HUP9800520A3 (en)	1999-09-28
CN1185180A (zh)	1998-06-17

Publication	Publication Date	Title
US4703008A (en)	1987-10-27	DNA sequences encoding erythropoietin
EP0668351B1 (en)	1999-09-22	Erythropoietin analogs
US5756349A (en)	1998-05-26	Production of erythropoietin
US5547933A (en)	1996-08-20	Production of erythropoietin
KR100361997B1 (ko)	2003-04-08	안정한살균/투과성-증가단백질산물및그것을포함하는제약학적조성물
US20080108560A1 (en)	2008-05-08	Heterologous G-Csf Fusion Proteins
EP2292650A1 (en)	2011-03-09	Methods and compositions for the prevention and treatment of anemia
US7098318B2 (en)	2006-08-29	Fusion protein having enhanced in vivo activity of erythropoietin
AU606585B2 (en)	1991-02-14	Human granulocyte-macrophage colony stimulating factor-like polypeptides and processes for producing them in high yields in microbial cells
US5545536A (en)	1996-08-13	Colony-stimulating factor derivatives
EP1809661B1 (en)	2011-05-18	Human interferon-beta mutein
AP730A (en)	1999-02-04	Gene expression in mammalian cells.
US20040254351A1 (en)	2004-12-16	Hyperglycosylated polypeptides
MXPA97007244A (en)	1998-11-12	Expression of genes in mamif cells
CA1339207C (en)	1997-08-05	The generation of recombinant eukaryotic cells with high-level expression
CA2453372A1 (en)	2003-02-13	Methylation resistant vectors
JP2798659B2 (ja)	1998-09-17	ヒトアンチトロンビンｉｉｉ（ａｔｉｉｉ）の製造
RU2261276C2 (ru)	2005-09-27	Выделенная молекула днк, кодирующая эритропоэтин человека, (варианты), экспрессирующий плазмидный или вирусный днк-вектор, гликопротеид эритропоэтин (варианты) и способ его получения, фармацевтическая композиция (варианты), линия клеток млекопитающего (варианты)
KR100512018B1 (ko)	2005-09-02	상동 재조합에 의해 인간 세포에서 인간 변이 단백질을 생성시키는 방법
AU4252400A (en)	2001-01-18	Production of erythropoietin
CZ443885A3 (en)	1996-09-11	Dna sequence used for assuring expression of polypeptide product
AU1974001A (en)	2001-05-03	Production of erythropoietin
HK1010398B (en)	2000-05-19	Erythropoietin analogs