IL115834A - Process for bacterial production of polypeptides - Google Patents
Process for bacterial production of polypeptidesInfo
- Publication number
- IL115834A IL115834A IL11583495A IL11583495A IL115834A IL 115834 A IL115834 A IL 115834A IL 11583495 A IL11583495 A IL 11583495A IL 11583495 A IL11583495 A IL 11583495A IL 115834 A IL115834 A IL 115834A
- Authority
- IL
- Israel
- Prior art keywords
- polypeptide
- nucleic acid
- dsba
- acid encoding
- protein
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 193
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 189
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 188
- 238000000034 method Methods 0.000 title claims abstract description 62
- 230000001580 bacterial effect Effects 0.000 title claims abstract description 30
- 230000008569 process Effects 0.000 title claims abstract description 29
- 238000004519 manufacturing process Methods 0.000 title description 14
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 111
- 210000004027 cell Anatomy 0.000 claims abstract description 88
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 66
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 65
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 64
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 64
- 230000014509 gene expression Effects 0.000 claims abstract description 35
- 241000894006 Bacteria Species 0.000 claims abstract description 33
- 210000001322 periplasm Anatomy 0.000 claims abstract description 25
- 239000001963 growth medium Substances 0.000 claims abstract description 23
- 239000002609 medium Substances 0.000 claims abstract description 17
- 230000001939 inductive effect Effects 0.000 claims abstract description 16
- 230000028327 secretion Effects 0.000 claims abstract description 14
- 108010076504 Protein Sorting Signals Proteins 0.000 claims abstract description 13
- 230000006698 induction Effects 0.000 claims abstract description 12
- 238000012258 culturing Methods 0.000 claims abstract description 6
- 235000018102 proteins Nutrition 0.000 claims description 59
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 claims description 46
- 239000013598 vector Substances 0.000 claims description 27
- 241000588724 Escherichia coli Species 0.000 claims description 25
- 230000000694 effects Effects 0.000 claims description 16
- 230000001965 increasing effect Effects 0.000 claims description 16
- 239000000411 inducer Substances 0.000 claims description 13
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 claims description 11
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 claims description 7
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 claims description 7
- 239000008101 lactose Substances 0.000 claims description 7
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 6
- 108010024636 Glutathione Proteins 0.000 claims description 5
- 108010090127 Periplasmic Proteins Proteins 0.000 claims description 5
- 230000003247 decreasing effect Effects 0.000 claims description 5
- 102000004195 Isomerases Human genes 0.000 claims description 4
- 108090000769 Isomerases Proteins 0.000 claims description 4
- 239000013604 expression vector Substances 0.000 claims description 4
- 239000006176 redox buffer Substances 0.000 claims description 4
- 235000001014 amino acid Nutrition 0.000 claims description 3
- 150000001413 amino acids Chemical class 0.000 claims description 3
- 241000588921 Enterobacteriaceae Species 0.000 claims description 2
- 102000013275 Somatomedins Human genes 0.000 claims description 2
- 229960003180 glutathione Drugs 0.000 claims description 2
- 241001112695 Clostridiales Species 0.000 claims 3
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 claims 1
- SRBFZHDQGSBBOR-HWQSCIPKSA-N L-arabinopyranose Chemical compound O[C@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-HWQSCIPKSA-N 0.000 claims 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical group CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 claims 1
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 description 44
- 239000012071 phase Substances 0.000 description 39
- 108020004414 DNA Proteins 0.000 description 27
- 101150009558 dsbA gene Proteins 0.000 description 27
- 239000013612 plasmid Substances 0.000 description 26
- 239000003795 chemical substances by application Substances 0.000 description 25
- 239000000872 buffer Substances 0.000 description 24
- 230000003196 chaotropic effect Effects 0.000 description 24
- 239000000047 product Substances 0.000 description 23
- 239000003638 chemical reducing agent Substances 0.000 description 21
- 230000035772 mutation Effects 0.000 description 20
- 239000012634 fragment Substances 0.000 description 19
- 241000894007 species Species 0.000 description 18
- 101100278567 Lelliottia amnigena dsbL gene Proteins 0.000 description 16
- 229920000642 polymer Polymers 0.000 description 15
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 14
- 101150015101 dsbC gene Proteins 0.000 description 14
- 150000003839 salts Chemical class 0.000 description 14
- 101150108812 proC gene Proteins 0.000 description 13
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 12
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 12
- 239000001301 oxygen Substances 0.000 description 12
- 229910052760 oxygen Inorganic materials 0.000 description 12
- 239000007787 solid Substances 0.000 description 12
- 239000002028 Biomass Substances 0.000 description 11
- 239000003153 chemical reaction reagent Substances 0.000 description 11
- 238000000855 fermentation Methods 0.000 description 11
- 230000004151 fermentation Effects 0.000 description 11
- 238000013518 transcription Methods 0.000 description 11
- 230000035897 transcription Effects 0.000 description 11
- 239000002904 solvent Substances 0.000 description 10
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 9
- 241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 9
- 229910052802 copper Inorganic materials 0.000 description 9
- 239000010949 copper Substances 0.000 description 9
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 8
- 101100407828 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) ptr-3 gene Proteins 0.000 description 8
- 108091028043 Nucleic acid sequence Proteins 0.000 description 8
- 229910019142 PO4 Inorganic materials 0.000 description 8
- 238000006664 bond formation reaction Methods 0.000 description 8
- 150000002696 manganese Chemical class 0.000 description 8
- 230000003287 optical effect Effects 0.000 description 8
- 230000002018 overexpression Effects 0.000 description 8
- 235000021317 phosphate Nutrition 0.000 description 8
- 239000004098 Tetracycline Substances 0.000 description 7
- 229960000723 ampicillin Drugs 0.000 description 7
- 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 7
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 7
- 239000004202 carbamide Substances 0.000 description 7
- 238000000605 extraction Methods 0.000 description 7
- 101150009573 phoA gene Proteins 0.000 description 7
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 7
- 239000010452 phosphate Substances 0.000 description 7
- 229960002180 tetracycline Drugs 0.000 description 7
- 229930101283 tetracycline Natural products 0.000 description 7
- 235000019364 tetracycline Nutrition 0.000 description 7
- 150000003522 tetracyclines Chemical class 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- 108090000099 Neurotrophin-4 Proteins 0.000 description 6
- 101100084022 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) lapA gene Proteins 0.000 description 6
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 238000010276 construction Methods 0.000 description 6
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 6
- 229940088598 enzyme Drugs 0.000 description 6
- 239000004615 ingredient Substances 0.000 description 6
- 229920001223 polyethylene glycol Polymers 0.000 description 6
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 5
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 5
- SRBFZHDQGSBBOR-SOOFDHNKSA-N D-ribopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@@H]1O SRBFZHDQGSBBOR-SOOFDHNKSA-N 0.000 description 5
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 5
- 108090000204 Dipeptidase 1 Proteins 0.000 description 5
- 101100178822 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) htrA1 gene Proteins 0.000 description 5
- 102000006010 Protein Disulfide-Isomerase Human genes 0.000 description 5
- 101100277437 Rhizobium meliloti (strain 1021) degP1 gene Proteins 0.000 description 5
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 5
- 229930006000 Sucrose Natural products 0.000 description 5
- 108091008874 T cell receptors Proteins 0.000 description 5
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 5
- 229910052783 alkali metal Inorganic materials 0.000 description 5
- 150000001340 alkali metals Chemical class 0.000 description 5
- 150000003863 ammonium salts Chemical class 0.000 description 5
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 5
- 235000018417 cysteine Nutrition 0.000 description 5
- 101150018266 degP gene Proteins 0.000 description 5
- 235000019441 ethanol Nutrition 0.000 description 5
- 238000004128 high performance liquid chromatography Methods 0.000 description 5
- -1 or NT-6) Proteins 0.000 description 5
- 238000012261 overproduction Methods 0.000 description 5
- 108020003519 protein disulfide isomerase Proteins 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 239000005720 sucrose Substances 0.000 description 5
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- 102000004594 DNA Polymerase I Human genes 0.000 description 4
- 108010017826 DNA Polymerase I Proteins 0.000 description 4
- 101100390711 Escherichia coli (strain K12) fhuA gene Proteins 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 108090001117 Insulin-Like Growth Factor II Proteins 0.000 description 4
- 102000048143 Insulin-Like Growth Factor II Human genes 0.000 description 4
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 4
- 108010025020 Nerve Growth Factor Proteins 0.000 description 4
- 102000035195 Peptidases Human genes 0.000 description 4
- 108091005804 Peptidases Proteins 0.000 description 4
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 4
- 238000009825 accumulation Methods 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 230000004186 co-expression Effects 0.000 description 4
- 239000000306 component Substances 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 229960000789 guanidine hydrochloride Drugs 0.000 description 4
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 238000007254 oxidation reaction Methods 0.000 description 4
- 230000010076 replication Effects 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 4
- 238000010361 transduction Methods 0.000 description 4
- 229910052723 transition metal Inorganic materials 0.000 description 4
- 239000004474 valine Substances 0.000 description 4
- 108091026890 Coding region Proteins 0.000 description 3
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
- 108010051696 Growth Hormone Proteins 0.000 description 3
- 102000018997 Growth Hormone Human genes 0.000 description 3
- 102000008100 Human Serum Albumin Human genes 0.000 description 3
- 108091006905 Human Serum Albumin Proteins 0.000 description 3
- 102000004877 Insulin Human genes 0.000 description 3
- 108090001061 Insulin Proteins 0.000 description 3
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 3
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 3
- 108090000742 Neurotrophin 3 Proteins 0.000 description 3
- 102100029268 Neurotrophin-3 Human genes 0.000 description 3
- 102000003683 Neurotrophin-4 Human genes 0.000 description 3
- 102100033857 Neurotrophin-4 Human genes 0.000 description 3
- 239000002202 Polyethylene glycol Substances 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 241000607142 Salmonella Species 0.000 description 3
- 102100033571 Tissue-type plasminogen activator Human genes 0.000 description 3
- 108050006955 Tissue-type plasminogen activator Proteins 0.000 description 3
- 108091023040 Transcription factor Proteins 0.000 description 3
- 102000040945 Transcription factor Human genes 0.000 description 3
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 3
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- 102000006635 beta-lactamase Human genes 0.000 description 3
- 239000003054 catalyst Substances 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 239000000122 growth hormone Substances 0.000 description 3
- 230000002209 hydrophobic effect Effects 0.000 description 3
- 101150020087 ilvG gene Proteins 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 238000000622 liquid--liquid extraction Methods 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 235000015097 nutrients Nutrition 0.000 description 3
- 230000003647 oxidation Effects 0.000 description 3
- 230000000704 physical effect Effects 0.000 description 3
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 3
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 3
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 3
- 239000013615 primer Substances 0.000 description 3
- 230000012846 protein folding Effects 0.000 description 3
- 230000003248 secreting effect Effects 0.000 description 3
- 238000000638 solvent extraction Methods 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- 229960005356 urokinase Drugs 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- INEWUCPYEUEQTN-UHFFFAOYSA-N 3-(cyclohexylamino)-2-hydroxy-1-propanesulfonic acid Chemical compound OS(=O)(=O)CC(O)CNC1CCCCC1 INEWUCPYEUEQTN-UHFFFAOYSA-N 0.000 description 2
- 229940122816 Amylase inhibitor Drugs 0.000 description 2
- 101100189062 Bacillus subtilis (strain 168) proH gene Proteins 0.000 description 2
- 102000007350 Bone Morphogenetic Proteins Human genes 0.000 description 2
- 108010007726 Bone Morphogenetic Proteins Proteins 0.000 description 2
- 102000004219 Brain-derived neurotrophic factor Human genes 0.000 description 2
- 108090000715 Brain-derived neurotrophic factor Proteins 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- 102100028892 Cardiotrophin-1 Human genes 0.000 description 2
- 102000007644 Colony-Stimulating Factors Human genes 0.000 description 2
- 108010071942 Colony-Stimulating Factors Proteins 0.000 description 2
- 102000016911 Deoxyribonucleases Human genes 0.000 description 2
- 108010053770 Deoxyribonucleases Proteins 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- 241001646716 Escherichia coli K-12 Species 0.000 description 2
- 241000206602 Eukaryota Species 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical class NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 238000010268 HPLC based assay Methods 0.000 description 2
- 108050008339 Heat Shock Transcription Factor Proteins 0.000 description 2
- 102000000039 Heat Shock Transcription Factor Human genes 0.000 description 2
- 102000002812 Heat-Shock Proteins Human genes 0.000 description 2
- 108010004889 Heat-Shock Proteins Proteins 0.000 description 2
- 101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 description 2
- 108090000144 Human Proteins Proteins 0.000 description 2
- 102000003839 Human Proteins Human genes 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 108010063738 Interleukins Proteins 0.000 description 2
- 102000015696 Interleukins Human genes 0.000 description 2
- 108010054278 Lac Repressors Proteins 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 102000005431 Molecular Chaperones Human genes 0.000 description 2
- 108010006519 Molecular Chaperones Proteins 0.000 description 2
- 102000015336 Nerve Growth Factor Human genes 0.000 description 2
- 102000007072 Nerve Growth Factors Human genes 0.000 description 2
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 2
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 2
- 108010076181 Proinsulin Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- 241000607720 Serratia Species 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- 101710142969 Somatoliberin Proteins 0.000 description 2
- 102100022831 Somatoliberin Human genes 0.000 description 2
- 101100288418 Staphylococcus xylosus lacP gene Proteins 0.000 description 2
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 2
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 2
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 2
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 2
- 108010009583 Transforming Growth Factors Proteins 0.000 description 2
- 102000009618 Transforming Growth Factors Human genes 0.000 description 2
- 101710162629 Trypsin inhibitor Proteins 0.000 description 2
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 2
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 2
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 229910052784 alkaline earth metal Inorganic materials 0.000 description 2
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 description 2
- 229940024606 amino acid Drugs 0.000 description 2
- 239000003392 amylase inhibitor Substances 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 239000003114 blood coagulation factor Substances 0.000 description 2
- 229940112869 bone morphogenetic protein Drugs 0.000 description 2
- 210000004556 brain Anatomy 0.000 description 2
- 229940077737 brain-derived neurotrophic factor Drugs 0.000 description 2
- 239000008366 buffered solution Substances 0.000 description 2
- OSGAYBCDTDRGGQ-UHFFFAOYSA-L calcium sulfate Chemical compound [Ca+2].[O-]S([O-])(=O)=O OSGAYBCDTDRGGQ-UHFFFAOYSA-L 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 108010041776 cardiotrophin 1 Proteins 0.000 description 2
- 150000001768 cations Chemical class 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 150000001860 citric acid derivatives Chemical class 0.000 description 2
- 229940047120 colony stimulating factors Drugs 0.000 description 2
- 230000001276 controlling effect Effects 0.000 description 2
- 229920001577 copolymer Polymers 0.000 description 2
- 101150071678 dsbB gene Proteins 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 238000000265 homogenisation Methods 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 229920001477 hydrophilic polymer Polymers 0.000 description 2
- 239000002596 immunotoxin Substances 0.000 description 2
- 231100000608 immunotoxin Toxicity 0.000 description 2
- 230000002637 immunotoxin Effects 0.000 description 2
- 229940051026 immunotoxin Drugs 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion 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
- 229940047122 interleukins Drugs 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 101150093139 ompT gene Proteins 0.000 description 2
- 239000003960 organic solvent Substances 0.000 description 2
- 230000000065 osmolyte Effects 0.000 description 2
- 230000001590 oxidative effect Effects 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 229920001451 polypropylene glycol Polymers 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 101150034869 rpo5 gene Proteins 0.000 description 2
- 101150106872 rpoH gene Proteins 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000001509 sodium citrate Substances 0.000 description 2
- 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 2
- 229910052938 sodium sulfate Inorganic materials 0.000 description 2
- 235000011152 sodium sulphate Nutrition 0.000 description 2
- 230000007928 solubilization Effects 0.000 description 2
- 238000005063 solubilization Methods 0.000 description 2
- 239000013589 supplement Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)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](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)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](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- 239000002753 trypsin inhibitor Substances 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 1
- FZWBNHMXJMCXLU-UHFFFAOYSA-N 2,3,4,5-tetrahydroxy-6-[3,4,5-trihydroxy-6-[[3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxymethyl]oxan-2-yl]oxyhexanal Chemical compound OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OCC(O)C(O)C(O)C(O)C=O)O1 FZWBNHMXJMCXLU-UHFFFAOYSA-N 0.000 description 1
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
- OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 108010059616 Activins Proteins 0.000 description 1
- 102000005606 Activins Human genes 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 239000004254 Ammonium phosphate Substances 0.000 description 1
- 108010005853 Anti-Mullerian Hormone Proteins 0.000 description 1
- 241000203069 Archaea Species 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241000589151 Azotobacter Species 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 108010077805 Bacterial Proteins Proteins 0.000 description 1
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 1
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 1
- 102000013585 Bombesin Human genes 0.000 description 1
- 108010051479 Bombesin Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108010009575 CD55 Antigens Proteins 0.000 description 1
- 102400000113 Calcitonin Human genes 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- OKTJSMMVPCPJKN-NJFSPNSNSA-N Carbon-14 Chemical compound [14C] OKTJSMMVPCPJKN-NJFSPNSNSA-N 0.000 description 1
- 206010007572 Cardiac hypertrophy Diseases 0.000 description 1
- 208000006029 Cardiomegaly Diseases 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 102000005572 Cathepsin A Human genes 0.000 description 1
- 108010059081 Cathepsin A Proteins 0.000 description 1
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- QNAYBMKLOCPYGJ-UWTATZPHSA-N D-alanine Chemical compound C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 244000078127 Eleusine coracana Species 0.000 description 1
- 235000013499 Eleusine coracana subsp coracana Nutrition 0.000 description 1
- 241000588914 Enterobacter Species 0.000 description 1
- BRLQWZUYTZBJKN-UHFFFAOYSA-N Epichlorohydrin Chemical compound ClCC1CO1 BRLQWZUYTZBJKN-UHFFFAOYSA-N 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 241000588698 Erwinia Species 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- 241001522878 Escherichia coli B Species 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 102000018233 Fibroblast Growth Factor Human genes 0.000 description 1
- 108050007372 Fibroblast Growth Factor Proteins 0.000 description 1
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 1
- 102100031706 Fibroblast growth factor 1 Human genes 0.000 description 1
- 102100024785 Fibroblast growth factor 2 Human genes 0.000 description 1
- 108090000379 Fibroblast growth factor 2 Proteins 0.000 description 1
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 description 1
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 102000006771 Gonadotropins Human genes 0.000 description 1
- 108010086677 Gonadotropins Proteins 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 1
- 101100082540 Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) pcp gene Proteins 0.000 description 1
- 101001072202 Homo sapiens Protein disulfide-isomerase Proteins 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 239000000854 Human Growth Hormone Substances 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
- 102100037852 Insulin-like growth factor I Human genes 0.000 description 1
- 102000006992 Interferon-alpha Human genes 0.000 description 1
- 108010047761 Interferon-alpha Proteins 0.000 description 1
- 102000003996 Interferon-beta Human genes 0.000 description 1
- 108090000467 Interferon-beta Proteins 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- 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 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 239000006137 Luria-Bertani broth Substances 0.000 description 1
- 102000009151 Luteinizing Hormone Human genes 0.000 description 1
- 108010073521 Luteinizing Hormone Proteins 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 229920002774 Maltodextrin Polymers 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 108090000028 Neprilysin Proteins 0.000 description 1
- 102000003729 Neprilysin Human genes 0.000 description 1
- 108090000095 Neurotrophin-6 Proteins 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 239000008118 PEG 6000 Substances 0.000 description 1
- 241001057811 Paracoccus <mealybug> Species 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 108010087702 Penicillinase Proteins 0.000 description 1
- 102000009658 Peptidylprolyl Isomerase Human genes 0.000 description 1
- 108010020062 Peptidylprolyl Isomerase Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 102000001938 Plasminogen Activators Human genes 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 229920001030 Polyethylene Glycol 4000 Polymers 0.000 description 1
- 229920002584 Polyethylene Glycol 6000 Polymers 0.000 description 1
- 229920002594 Polyethylene Glycol 8000 Polymers 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- 241000588769 Proteus <enterobacteria> Species 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 102000004879 Racemases and epimerases Human genes 0.000 description 1
- 108090001066 Racemases and epimerases Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108090000103 Relaxin Proteins 0.000 description 1
- 102000003743 Relaxin Human genes 0.000 description 1
- 102400000834 Relaxin A chain Human genes 0.000 description 1
- 101800000074 Relaxin A chain Proteins 0.000 description 1
- 102400000610 Relaxin B chain Human genes 0.000 description 1
- 101710109558 Relaxin B chain Proteins 0.000 description 1
- 108090000783 Renin Proteins 0.000 description 1
- 102100028255 Renin Human genes 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102400000827 Saposin-D Human genes 0.000 description 1
- 101800001700 Saposin-D Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 241000607768 Shigella Species 0.000 description 1
- 108010063499 Sigma Factor Proteins 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- NINIDFKCEFEMDL-AKLPVKDBSA-N Sulfur-35 Chemical compound [35S] NINIDFKCEFEMDL-AKLPVKDBSA-N 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 241000473945 Theria <moth genus> Species 0.000 description 1
- ZMZDMBWJUHKJPS-UHFFFAOYSA-M Thiocyanate anion Chemical class [S-]C#N ZMZDMBWJUHKJPS-UHFFFAOYSA-M 0.000 description 1
- 102000002933 Thioredoxin Human genes 0.000 description 1
- 101710159478 Thioredoxin-like protein Proteins 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 108010000499 Thromboplastin Proteins 0.000 description 1
- 102000002262 Thromboplastin Human genes 0.000 description 1
- 102000036693 Thrombopoietin Human genes 0.000 description 1
- 108010041111 Thrombopoietin Proteins 0.000 description 1
- 102000011923 Thyrotropin Human genes 0.000 description 1
- 108010061174 Thyrotropin Proteins 0.000 description 1
- 102400001320 Transforming growth factor alpha Human genes 0.000 description 1
- 101800004564 Transforming growth factor alpha Proteins 0.000 description 1
- YZCKVEUIGOORGS-NJFSPNSNSA-N Tritium Chemical compound [3H] YZCKVEUIGOORGS-NJFSPNSNSA-N 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 241000863000 Vitreoscilla Species 0.000 description 1
- 239000000488 activin Substances 0.000 description 1
- 230000001476 alcoholic effect Effects 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 150000001342 alkaline earth metals Chemical class 0.000 description 1
- 229910000148 ammonium phosphate Inorganic materials 0.000 description 1
- 235000019289 ammonium phosphates Nutrition 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000001455 anti-clotting effect Effects 0.000 description 1
- 239000000868 anti-mullerian hormone Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 150000001479 arabinose derivatives Chemical class 0.000 description 1
- 230000001746 atrial effect Effects 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 230000010310 bacterial transformation Effects 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- DNDCVAGJPBKION-DOPDSADYSA-N bombesin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1NC2=CC=CC=C2C=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1NC(=O)CC1)C(C)C)C1=CN=CN1 DNDCVAGJPBKION-DOPDSADYSA-N 0.000 description 1
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 230000005587 bubbling Effects 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 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
- 235000011132 calcium sulphate Nutrition 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 239000003729 cation exchange resin Substances 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 108091092328 cellular RNA Proteins 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000011098 chromatofocusing Methods 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 239000003398 denaturant Substances 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000009795 derivation Methods 0.000 description 1
- 229940119743 dextran 70 Drugs 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- MNNHAPBLZZVQHP-UHFFFAOYSA-N diammonium hydrogen phosphate Chemical compound [NH4+].[NH4+].OP([O-])([O-])=O MNNHAPBLZZVQHP-UHFFFAOYSA-N 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 229910001882 dioxygen Inorganic materials 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229960004222 factor ix Drugs 0.000 description 1
- 229940126864 fibroblast growth factor Drugs 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 229940028334 follicle stimulating hormone Drugs 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 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 1
- 229960004666 glucagon Drugs 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000002622 gonadotropin Substances 0.000 description 1
- 229960004198 guanidine Drugs 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 108010067006 heat stable toxin (E coli) Proteins 0.000 description 1
- 230000002607 hemopoietic effect Effects 0.000 description 1
- 102000044162 human IGF1 Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- ZMZDMBWJUHKJPS-UHFFFAOYSA-N hydrogen thiocyanate Chemical class SC#N ZMZDMBWJUHKJPS-UHFFFAOYSA-N 0.000 description 1
- CPSYWNLKRDURMG-UHFFFAOYSA-L hydron;manganese(2+);phosphate Chemical compound [Mn+2].OP([O-])([O-])=O CPSYWNLKRDURMG-UHFFFAOYSA-L 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000010324 immunological assay Methods 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 239000000893 inhibin Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 102000028416 insulin-like growth factor binding Human genes 0.000 description 1
- 108091022911 insulin-like growth factor binding Proteins 0.000 description 1
- 102000006495 integrins Human genes 0.000 description 1
- 108010044426 integrins Proteins 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 238000006317 isomerization reaction Methods 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- 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 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 101150074251 lpp gene Proteins 0.000 description 1
- 229940066294 lung surfactant Drugs 0.000 description 1
- 239000003580 lung surfactant Substances 0.000 description 1
- 229940040129 luteinizing hormone Drugs 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- GVALZJMUIHGIMD-UHFFFAOYSA-H magnesium phosphate Chemical compound [Mg+2].[Mg+2].[Mg+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O GVALZJMUIHGIMD-UHFFFAOYSA-H 0.000 description 1
- 239000004137 magnesium phosphate Substances 0.000 description 1
- 229910000157 magnesium phosphate Inorganic materials 0.000 description 1
- 229960002261 magnesium phosphate Drugs 0.000 description 1
- 235000010994 magnesium phosphates Nutrition 0.000 description 1
- 159000000003 magnesium salts Chemical class 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 229940099596 manganese sulfate Drugs 0.000 description 1
- 239000011702 manganese sulphate Substances 0.000 description 1
- 235000007079 manganese sulphate Nutrition 0.000 description 1
- SQQMAOCOWKFBNP-UHFFFAOYSA-L manganese(II) sulfate Chemical compound [Mn+2].[O-]S([O-])(=O)=O SQQMAOCOWKFBNP-UHFFFAOYSA-L 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000012533 medium component Substances 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 229940053128 nerve growth factor Drugs 0.000 description 1
- 239000003900 neurotrophic factor Substances 0.000 description 1
- 229940032018 neurotrophin 3 Drugs 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000011330 nucleic acid test Methods 0.000 description 1
- 230000002138 osteoinductive effect Effects 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- 239000000199 parathyroid hormone Substances 0.000 description 1
- 229960001319 parathyroid hormone Drugs 0.000 description 1
- 238000005192 partition Methods 0.000 description 1
- 229950009506 penicillinase Drugs 0.000 description 1
- 239000012466 permeate Substances 0.000 description 1
- 238000010587 phase diagram Methods 0.000 description 1
- 101150078860 pho gene Proteins 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 230000004983 pleiotropic effect Effects 0.000 description 1
- 239000003880 polar aprotic solvent Substances 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 235000019422 polyvinyl alcohol Nutrition 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 229960003975 potassium Drugs 0.000 description 1
- 239000001508 potassium citrate Substances 0.000 description 1
- 229960002635 potassium citrate Drugs 0.000 description 1
- QEEAPRPFLLJWCF-UHFFFAOYSA-K potassium citrate (anhydrous) Chemical compound [K+].[K+].[K+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O QEEAPRPFLLJWCF-UHFFFAOYSA-K 0.000 description 1
- 235000011082 potassium citrates Nutrition 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- OTYBMLCTZGSZBG-UHFFFAOYSA-L potassium sulfate Chemical compound [K+].[K+].[O-]S([O-])(=O)=O OTYBMLCTZGSZBG-UHFFFAOYSA-L 0.000 description 1
- 229910052939 potassium sulfate Inorganic materials 0.000 description 1
- 235000011151 potassium sulphates Nutrition 0.000 description 1
- 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 1
- 238000002360 preparation method Methods 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 108010087851 prorelaxin Proteins 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 235000002079 ragi Nutrition 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 230000000754 repressing effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000027756 respiratory electron transport chain Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000012279 sodium borohydride Substances 0.000 description 1
- 229910000033 sodium borohydride Inorganic materials 0.000 description 1
- 235000011083 sodium citrates Nutrition 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 235000011008 sodium phosphates Nutrition 0.000 description 1
- VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229940071127 thioglycolate Drugs 0.000 description 1
- CWERGRDVMFNCDR-UHFFFAOYSA-M thioglycolate(1-) Chemical compound [O-]C(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-M 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 229960000187 tissue plasminogen activator Drugs 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 150000003624 transition metals Chemical class 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
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 229910052722 tritium Inorganic materials 0.000 description 1
- 108010087967 type I signal peptidase Proteins 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 210000005253 yeast cell Anatomy 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0051—Oxidoreductases (1.) acting on a sulfur group of donors (1.8)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1133—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by redox-reactions involving cystein/cystin side chains
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—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
- C07K14/245—Escherichia (G)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/65—Insulin-like growth factors, i.e. somatomedins, e.g. IGF-1, IGF-2
-
- 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
- C12N15/70—Vectors or expression systems specially adapted for E. coli
-
- 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
- C12N9/90—Isomerases (5.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- General Engineering & Computer Science (AREA)
- Biophysics (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Analytical Chemistry (AREA)
- Diabetes (AREA)
- Endocrinology (AREA)
- Toxicology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/333,912 US5639635A (en) | 1994-11-03 | 1994-11-03 | Process for bacterial production of polypeptides |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IL115834A0 IL115834A0 (en) | 1996-01-19 |
| IL115834A true IL115834A (en) | 2004-08-31 |
Family
ID=23304776
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL11583495A IL115834A (en) | 1994-11-03 | 1995-10-31 | Process for bacterial production of polypeptides |
Country Status (11)
| Country | Link |
|---|---|
| US (1) | US5639635A (es) |
| EP (1) | EP0786009B1 (es) |
| JP (1) | JP3749257B2 (es) |
| AT (1) | ATE318917T1 (es) |
| CA (1) | CA2203373C (es) |
| DE (1) | DE69534822T2 (es) |
| DK (1) | DK0786009T3 (es) |
| ES (1) | ES2259440T3 (es) |
| IL (1) | IL115834A (es) |
| MX (1) | MX9703012A (es) |
| WO (1) | WO1996014422A1 (es) |
Families Citing this family (155)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5789199A (en) * | 1994-11-03 | 1998-08-04 | Genentech, Inc. | Process for bacterial production of polypeptides |
| DE19604583C2 (de) * | 1996-02-08 | 1999-11-18 | Fraunhofer Ges Forschung | Verfahren zur Synthese von löslichen, rekombinanten Proteinen aus Bakterienzellen |
| US6027888A (en) * | 1996-04-05 | 2000-02-22 | Board Of Regents, The University Of Texas System | Methods for producing soluble, biologically-active disulfide-bond containing eukaryotic proteins in bacterial cells |
| US6083715A (en) * | 1997-06-09 | 2000-07-04 | Board Of Regents, The University Of Texas System | Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells |
| US6361964B1 (en) | 1997-08-12 | 2002-03-26 | Massachusetts Institute Of Technology | Eukaryotic disulfide bond-forming proteins and related molecules and methods |
| DE69842019D1 (de) * | 1997-10-16 | 2011-01-05 | Synageva Biopharma Corp | Transgene vögel und proteinproduktion |
| DE19749259A1 (de) * | 1997-11-07 | 1999-05-12 | Dade Behring Marburg Gmbh | Verfahren zur Herstellung von funktionalem rekombinantem Gewebsfaktor |
| WO2000002996A2 (en) | 1998-07-10 | 2000-01-20 | Cornell Research Foundation, Inc. | Recombinant constructs and systems for secretion of proteins via type iii secretion systems |
| JP2000083670A (ja) * | 1998-09-09 | 2000-03-28 | Hsp Kenkyusho:Kk | ＤｓｂＡ／ＤｓｂＢ／ＤｓｂＣ／ＤｓｂＤ発現プラスミド |
| EP1048732A1 (de) | 1999-04-26 | 2000-11-02 | F. Hoffmann-La Roche Ag | Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen |
| FI109361B (fi) | 1999-05-04 | 2002-07-15 | Korpela Timo | Mikrobinen proteiinin ilmentämisjärjestelmä |
| EP1077263A1 (de) * | 1999-07-29 | 2001-02-21 | F.Hoffmann-La Roche Ag | Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen durch Co-Sekretion von Chaperonen |
| US6808902B1 (en) * | 1999-11-12 | 2004-10-26 | Amgen Inc. | Process for correction of a disulfide misfold in IL-1Ra Fc fusion molecules |
| ES2324645T3 (es) | 2000-11-03 | 2009-08-12 | Genentech, Inc. | Cambios de tasa metabolica en fermentaciones que expresen proteinas recombinantes. |
| US6979556B2 (en) * | 2000-12-14 | 2005-12-27 | Genentech, Inc. | Separate-cistron contructs for secretion of aglycosylated antibodies from prokaryotes |
| US20030077739A1 (en) * | 2001-08-27 | 2003-04-24 | Genentech, Inc. | System for antibody expression and assembly |
| CN100552023C (zh) * | 2001-09-13 | 2009-10-21 | 杰南技术公司 | 氨肽酶 |
| WO2004042017A2 (en) * | 2002-10-31 | 2004-05-21 | Genentech, Inc. | Methods and compositions for increasing antibody production |
| AU2004205684A1 (en) * | 2003-01-23 | 2004-08-05 | Genentech, Inc. | Methods for producing humanized antibodies and improving yield of antibodies or antigen binding fragments in cell culture |
| CA2534055A1 (en) * | 2003-08-01 | 2005-02-10 | Genentech, Inc. | Antibody cdr polypeptide sequences with restricted diversity |
| EP1663306A2 (en) * | 2003-09-05 | 2006-06-07 | Genentech, Inc. | Antibodies with altered effector functions |
| NZ547438A (en) | 2003-12-19 | 2010-01-29 | Genentech Inc | Monovalent antibody fragments useful as therapeutics |
| US7300776B2 (en) | 2004-04-26 | 2007-11-27 | Ajinomoto Co., Inc. | L-amino acid-producing bacterium and a method for producing L-amino acid |
| MX2007002856A (es) * | 2004-09-02 | 2007-09-25 | Genentech Inc | Metodos para el uso de ligandos receptores de muerte y anticuerpos c20. |
| CN101094868B (zh) | 2004-09-03 | 2013-07-10 | 健泰科生物技术公司 | 人源化的抗-β7拮抗剂及其应用 |
| US8137928B2 (en) | 2005-03-24 | 2012-03-20 | BioGeneriX | Expression of soluble, active eukaryotic glycosyltransferases in prokaryotic organisms |
| US20070026012A1 (en) | 2005-08-01 | 2007-02-01 | Cornell Research Foundation, Inc. | Compositions and methods for monitoring and altering protein folding and solubility |
| AU2006283130B2 (en) | 2005-08-22 | 2012-02-09 | Cornell Research Foundation, Inc. | Compositions and methods for analyzing protein interactions |
| US8679490B2 (en) | 2005-11-07 | 2014-03-25 | Genentech, Inc. | Binding polypeptides with diversified and consensus VH/VL hypervariable sequences |
| BRPI0619118A2 (pt) | 2005-12-02 | 2011-09-13 | Genentech Inc | composições e métodos para o tratamento de doenças e desordens associadas com a sinalização de citocina |
| JP5808070B2 (ja) * | 2005-12-02 | 2015-11-10 | ジェネンテック， インコーポレイテッド | 結合ポリペプチド及びその使用 |
| WO2007120334A2 (en) | 2005-12-15 | 2007-10-25 | Genentech, Inc. | Methods and compositions for targeting polyubiquitin |
| AU2007248444B2 (en) | 2006-01-05 | 2012-10-25 | Genentech, Inc. | Anti-EphB4 antibodies and methods using same |
| AR059851A1 (es) | 2006-03-16 | 2008-04-30 | Genentech Inc | Anticuerpos de la egfl7 y metodos de uso |
| WO2007136463A2 (en) * | 2006-04-07 | 2007-11-29 | Dow Global Technologies Incorporated | Processes for improved disulfide bond formation in recombinant systems |
| WO2007127589A2 (en) * | 2006-04-07 | 2007-11-08 | The Board Of Regents Of The University Of Texas System | Artificial disulfide isomerases and uses thereof |
| CN103030696B (zh) | 2006-05-30 | 2016-09-28 | 健泰科生物技术公司 | 抗体和免疫偶联物及其用途 |
| PL2845866T3 (pl) | 2006-10-27 | 2017-10-31 | Genentech Inc | Przeciwciała i immunokoniugaty oraz ich zastosowanie |
| US20100119526A1 (en) * | 2007-01-26 | 2010-05-13 | Bioinvent International Ab | DLL4 Signaling Inhibitors and Uses Thereof |
| US7960139B2 (en) | 2007-03-23 | 2011-06-14 | Academia Sinica | Alkynyl sugar analogs for the labeling and visualization of glycoconjugates in cells |
| PE20090321A1 (es) | 2007-06-04 | 2009-04-20 | Genentech Inc | Anticuerpos anti-notch1 nrr, metodo de preparacion y composicion farmaceutica |
| KR20190140090A (ko) | 2007-07-09 | 2019-12-18 | 제넨테크, 인크. | 폴리펩티드의 재조합 생산 동안의 디술피드 결합 환원의 방지 |
| AU2008276128B2 (en) | 2007-07-16 | 2013-10-10 | Genentech, Inc. | Humanized anti-CD79b antibodies and immunoconjugates and methods of use |
| CL2008002085A1 (es) | 2007-07-16 | 2008-11-21 | Genentech Inc | Anticuerpo humanizado anti-cd79b/igbeta/b29; polinucleotido codificacnte, vector, celula huesped; metodo de fabricacion; inmunoconjugado; composicion farmaceutica; uso para tratar cancer; metodo in vitro para determinar presencia de cd79b, oinhibir crecimiento de celulas quqe expresa cd79b; ensayo in vitro para detectar celulas b |
| CN104888193A (zh) | 2007-11-07 | 2015-09-09 | 健泰科生物技术公司 | 用于治疗微生物病症的组合物和方法 |
| HUE029869T2 (en) | 2008-01-31 | 2017-04-28 | Genentech Inc | Anti-CD79B antibodies and immunoconjugates, as well as application procedures |
| CR20170001A (es) | 2008-04-28 | 2017-08-10 | Genentech Inc | Anticuerpos anti factor d humanizados |
| WO2010009271A2 (en) | 2008-07-15 | 2010-01-21 | Academia Sinica | Glycan arrays on ptfe-like aluminum coated glass slides and related methods |
| KR20190069615A (ko) | 2008-12-09 | 2019-06-19 | 제넨테크, 인크. | 항-ｐｄ-ｌ１ 항체 및 ｔ 세포 기능을 향상시키기 위한 그의 용도 |
| MA33208B1 (fr) | 2009-03-25 | 2012-04-02 | Genentech Inc | Anticorps anti-fgfr3 et procédés d'utilisation de ceux-ci |
| CN102471380B (zh) | 2009-04-01 | 2015-01-14 | 霍夫曼-拉罗奇有限公司 | 抗FcRH5抗体和免疫偶联物及使用方法 |
| KR101431318B1 (ko) | 2009-04-02 | 2014-08-20 | 로슈 글리카트 아게 | 전장 항체 및 단일쇄 ｆａｂ 단편을 포함하는 다중특이성 항체 |
| SG10201408401RA (en) | 2009-09-16 | 2015-01-29 | Genentech Inc | Coiled coil and/or tether containing protein complexes and uses thereof |
| US20110206704A1 (en) * | 2009-10-19 | 2011-08-25 | Genentech, Inc. | Methods and compositions for modulating hepatocyte growth factor activator |
| BR112012009245A2 (pt) | 2009-10-19 | 2019-09-24 | Genentech Inc | ''anticorpo,polinucleotídeo,celula hospedeira,método para fabricar um anticorpo,imunoconjugado,formulação farmacêutica e uso do anticorpo'' |
| WO2011050188A1 (en) | 2009-10-22 | 2011-04-28 | Genentech, Inc. | Anti-hepsin antibodies and methods using same |
| WO2011056502A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Bone morphogenetic protein receptor type ii compositions and methods of use |
| WO2011056494A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Activin receptor-like kinase-1 antagonist and vegfr3 antagonist combinations |
| WO2011056497A1 (en) | 2009-10-26 | 2011-05-12 | Genentech, Inc. | Activin receptor type iib compositions and methods of use |
| EP2496601B1 (en) | 2009-11-05 | 2017-06-07 | F. Hoffmann-La Roche AG | Methods and composition for secretion of heterologous polypeptides |
| US11377485B2 (en) | 2009-12-02 | 2022-07-05 | Academia Sinica | Methods for modifying human antibodies by glycan engineering |
| US10087236B2 (en) | 2009-12-02 | 2018-10-02 | Academia Sinica | Methods for modifying human antibodies by glycan engineering |
| RU2559542C2 (ru) | 2009-12-23 | 2015-08-10 | Дженентек, Инк. | Антитела против bv8 и их применение |
| GB201000590D0 (en) | 2010-01-14 | 2010-03-03 | Ucb Pharma Sa | Bacterial host strain |
| GB201000588D0 (en) | 2010-01-14 | 2010-03-03 | Ucb Pharma Sa | Bacterial host strain |
| GB201000591D0 (en) | 2010-01-14 | 2010-03-03 | Ucb Pharma Sa | Bacterial hoist strain |
| US20110262903A1 (en) | 2010-02-26 | 2011-10-27 | Life Technologies Corporation | Modified Proteins and Methods of Making and Using Same |
| US20130045871A1 (en) | 2010-03-18 | 2013-02-21 | Cornell University | Engineering correctly folded antibodies using inner membrane display of twin-arginine translocation intermediates |
| AR080793A1 (es) | 2010-03-26 | 2012-05-09 | Roche Glycart Ag | Anticuerpos biespecificos |
| WO2011130332A1 (en) | 2010-04-12 | 2011-10-20 | Academia Sinica | Glycan arrays for high throughput screening of viruses |
| EP2560683B2 (en) | 2010-04-23 | 2022-07-20 | F. Hoffmann-La Roche AG | Production of heteromultimeric proteins |
| CA2795972A1 (en) | 2010-06-03 | 2011-12-08 | Genentech, Inc. | Immuno-pet imaging of antibodies and immunoconjugates and uses therefor |
| JP5758004B2 (ja) | 2010-08-24 | 2015-08-05 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | ジスルフィドによって安定化されたＦｖ断片を含む二重特異性抗体 |
| GB201018664D0 (en) | 2010-11-05 | 2010-12-22 | Msd Biolog Uk Ltd | Expression process |
| JP5766296B2 (ja) | 2010-12-23 | 2015-08-19 | エフ．ホフマン−ラ ロシュ アーゲーＦ． Ｈｏｆｆｍａｎｎ−Ｌａ Ｒｏｃｈｅ Ａｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ | ポリペプチド−ポリヌクレオチド複合体、およびエフェクター成分の標的化された送達におけるその使用 |
| WO2012092539A2 (en) | 2010-12-31 | 2012-07-05 | Takeda Pharmaceutical Company Limited | Antibodies to dll4 and uses thereof |
| EP2670776B1 (en) | 2011-02-04 | 2018-11-21 | F. Hoffmann-La Roche AG | Fc VARIANTS AND METHODS FOR THEIR PRODUCTION |
| US10689447B2 (en) | 2011-02-04 | 2020-06-23 | Genentech, Inc. | Fc variants and methods for their production |
| EP2546267A1 (en) | 2011-07-13 | 2013-01-16 | UCB Pharma S.A. | Bacterial host strain expressing recombinant DsbC |
| SG10201807560XA (en) | 2011-07-13 | 2018-10-30 | Ucb Pharma Sa | Bacterial host strain expressing recombinant dsbc |
| SI2766397T1 (sl) | 2011-10-11 | 2018-09-28 | F. Hoffmann-La Roche Ag | Izboljšano sestavljanje bispecifičnih protiteles |
| EP2812357B1 (en) | 2012-02-10 | 2020-11-04 | F.Hoffmann-La Roche Ag | Single-chain antibodies and other heteromultimers |
| US9139863B2 (en) | 2012-03-16 | 2015-09-22 | Genentech, Inc. | Engineered conformationally-stabilized proteins |
| MX365947B (es) | 2012-03-27 | 2019-06-19 | Genentech Inc | Operaciones de cosecha mejoradas para proteinas recombinadas. |
| US10130714B2 (en) | 2012-04-14 | 2018-11-20 | Academia Sinica | Enhanced anti-influenza agents conjugated with anti-inflammatory activity |
| MX354862B (es) | 2012-06-27 | 2018-03-23 | Hoffmann La Roche | Método para la producción de entidades dirigidas altamente selectivas hechas a la medida y biespecíficas que contienen dos entidades de unión diferentes. |
| CA2871882A1 (en) | 2012-06-27 | 2014-01-03 | F. Hoffmann-La Roche Ag | Method for making antibody fc-region conjugates comprising at least one binding entity that specifically binds to a target and uses thereof |
| EP2885311B1 (en) | 2012-08-18 | 2020-01-01 | Academia Sinica | Cell-permeable probes for identification and imaging of sialidases |
| US10086054B2 (en) | 2013-06-26 | 2018-10-02 | Academia Sinica | RM2 antigens and use thereof |
| WO2014210564A1 (en) | 2013-06-27 | 2014-12-31 | Academia Sinica | Glycan conjugates and use thereof |
| JP6486368B2 (ja) | 2013-09-06 | 2019-03-20 | アカデミア シニカＡｃａｄｅｍｉａ Ｓｉｎｉｃａ | 改変されたグリコシル基を含む糖脂質を用いたヒトｉＮＫＴ細胞の活性化 |
| CN105934252B (zh) | 2013-10-10 | 2020-11-10 | 贝思以色列女会吏医学中心公司 | Tm4sf1结合蛋白及其使用方法 |
| LT3079719T (lt) | 2013-12-09 | 2019-12-10 | Allakos Inc | Antikūnai prieš siglec-8 ir jų panaudojimo būdai |
| US10150818B2 (en) | 2014-01-16 | 2018-12-11 | Academia Sinica | Compositions and methods for treatment and detection of cancers |
| WO2016114819A1 (en) | 2015-01-16 | 2016-07-21 | Academia Sinica | Compositions and methods for treatment and detection of cancers |
| CA2937123A1 (en) | 2014-01-16 | 2015-07-23 | Academia Sinica | Compositions and methods for treatment and detection of cancers |
| CA2939931A1 (en) | 2014-02-28 | 2015-09-03 | Christopher Robert Bebbington | Methods and compositions for treating siglec-8 associated diseases |
| JP6644717B2 (ja) | 2014-03-14 | 2020-02-12 | ジェネンテック， インコーポレイテッド | 異種ポリペプチドを分泌させるための方法及び組成物 |
| JP6562942B2 (ja) | 2014-03-27 | 2019-08-28 | アカデミア シニカＡｃａｄｅｍｉａ Ｓｉｎｉｃａ | 反応性標識化合物およびその使用 |
| EP3140392B1 (en) | 2014-05-06 | 2023-07-26 | F. Hoffmann-La Roche AG | Production of heteromultimeric proteins using mammalian cells |
| CA2950440A1 (en) | 2014-05-27 | 2015-12-03 | Academia Sinica | Anti-her2 glycoantibodies and uses thereof |
| US10118969B2 (en) | 2014-05-27 | 2018-11-06 | Academia Sinica | Compositions and methods relating to universal glycoforms for enhanced antibody efficacy |
| KR20230033737A (ko) | 2014-05-27 | 2023-03-08 | 아카데미아 시니카 | 증진된 항체 효능을 위한 범용 당형태에 관한 조성물 및 방법 |
| KR20240096599A (ko) | 2014-05-27 | 2024-06-26 | 아카데미아 시니카 | 항-ｃｄ20 글리코항체 및 이의 용도 |
| JP7063538B2 (ja) | 2014-05-28 | 2022-05-09 | アカデミア シニカ | 抗ＴＮＦα糖操作抗体群およびその使用 |
| US10328149B2 (en) | 2014-06-13 | 2019-06-25 | Tenboron Oy | Conjugates comprising an anti-EGFR1 antibody |
| US9879042B2 (en) | 2014-09-08 | 2018-01-30 | Academia Sinica | Human iNKT cell activation using glycolipids |
| CA2961439A1 (en) | 2014-11-05 | 2016-05-12 | Genentech, Inc. | Anti-fgfr2/3 antibodies and methods using same |
| CN107001482B (zh) | 2014-12-03 | 2021-06-15 | 豪夫迈·罗氏有限公司 | 多特异性抗体 |
| US9975965B2 (en) | 2015-01-16 | 2018-05-22 | Academia Sinica | Compositions and methods for treatment and detection of cancers |
| US10495645B2 (en) | 2015-01-16 | 2019-12-03 | Academia Sinica | Cancer markers and methods of use thereof |
| KR102691114B1 (ko) | 2015-01-24 | 2024-08-01 | 아카데미아 시니카 | 신규한 글리칸 콘주게이트 및 이를 사용하는 방법 |
| AU2016209056B2 (en) | 2015-01-24 | 2021-01-28 | Academia Sinica | Cancer markers and methods of use thereof |
| ES2901173T3 (es) | 2015-01-30 | 2022-03-21 | Academia Sinica | Composiciones y procedimientos relacionados con glicoformas universales para una eficacia de anticuerpos anti-SSEA4 mejorada |
| AU2016230018A1 (en) * | 2015-03-06 | 2017-09-21 | Genentech, Inc. | Ultrapurified DsbA and DsbC and methods of making and using the same |
| CA2981183A1 (en) | 2015-04-07 | 2016-10-13 | Greg Lazar | Antigen binding complex having agonistic activity and methods of use |
| CA2987797A1 (en) | 2015-06-17 | 2016-12-22 | Christopher Robert Bebbington | Methods and compositions for treating fibrotic diseases |
| CN105384825B (zh) | 2015-08-11 | 2018-06-01 | 南京传奇生物科技有限公司 | 一种基于单域抗体的双特异性嵌合抗原受体及其应用 |
| CN108026180B (zh) | 2015-08-28 | 2022-06-07 | 豪夫迈·罗氏有限公司 | 抗羟腐胺赖氨酸抗体及其用途 |
| US10604577B2 (en) | 2015-10-22 | 2020-03-31 | Allakos Inc. | Methods and compositions for treating systemic mastocytosis |
| KR20180114210A (ko) | 2016-03-08 | 2018-10-17 | 아카데미아 시니카 | N-글리칸의 모듈 합성 방법 및 그의 어레이 |
| MX2018014047A (es) | 2016-05-17 | 2019-06-20 | Genentech Inc | Firmas de genes estromales para el diagnóstico y uso en inmunoterapia. |
| BR112018075516A2 (pt) | 2016-06-17 | 2019-10-01 | Genentech Inc | purificação de anticorpos multiespecíficos |
| WO2018014260A1 (en) | 2016-07-20 | 2018-01-25 | Nanjing Legend Biotech Co., Ltd. | Multispecific antigen binding proteins and methods of use thereof |
| JP2019530434A (ja) | 2016-08-05 | 2019-10-24 | ジェネンテック， インコーポレイテッド | アゴニスト活性を有する多価及び多重エピトープ抗体ならびに使用方法 |
| US10538592B2 (en) | 2016-08-22 | 2020-01-21 | Cho Pharma, Inc. | Antibodies, binding fragments, and methods of use |
| WO2018049083A1 (en) | 2016-09-07 | 2018-03-15 | The Regents Of The University Of California | Antibodies to oxidation-specific epitopes |
| WO2018068201A1 (en) | 2016-10-11 | 2018-04-19 | Nanjing Legend Biotech Co., Ltd. | Single-domain antibodies and variants thereof against ctla-4 |
| JP2020500508A (ja) | 2016-10-28 | 2020-01-16 | バンヤン・バイオマーカーズ・インコーポレーテッド | ユビキチンｃ末端ヒドロラーゼｌ１（ｕｃｈ−ｌ１）およびグリア線維酸性タンパク質（ｇｆａｐ）に対する抗体および関連する方法 |
| AU2018261887A1 (en) | 2017-05-05 | 2019-12-05 | Allakos Inc. | Methods and compositions for treating allergic ocular diseases |
| CA3078974A1 (en) | 2017-10-12 | 2019-04-18 | Immunowake Inc. | Vegfr-antibody light chain fusion protein |
| JP7403164B2 (ja) | 2017-10-26 | 2023-12-22 | ザ リージェンツ オブ ザ ユニバーシティ オブ カリフォルニア | 虚血性再灌流障害を治療するための酸化特異的エピトープの阻害 |
| SG11202004158QA (en) | 2017-12-28 | 2020-06-29 | Nanjing Legend Biotech Co Ltd | Single-domain antibodies and variants thereof against tigit |
| CN111699200B (zh) | 2018-01-15 | 2023-05-26 | 南京传奇生物科技有限公司 | 针对pd-1的单域抗体和其变体 |
| CA3093034A1 (en) | 2018-03-30 | 2019-10-03 | Nanjing Legend Biotech Co., Ltd. | Single-domain antibodies against lag-3 and uses thereof |
| WO2019213331A1 (en) | 2018-05-01 | 2019-11-07 | Ambrx, Inc. | A method for optimizing antibody expression |
| WO2019214988A1 (en) * | 2018-05-11 | 2019-11-14 | Qiagen Gmbh | Lysis method for plant samples |
| EP4242238A3 (en) | 2018-05-14 | 2023-12-06 | Werewolf Therapeutics, Inc. | Activatable interleukin-2 polypeptides and methods of use thereof |
| KR20210021468A (ko) | 2018-05-14 | 2021-02-26 | 웨어울프 세라퓨틱스, 인크. | 활성화가능한 사이토카인 폴리펩타이드 및 이의 사용 방법 |
| AU2019347751A1 (en) | 2018-09-27 | 2021-04-29 | Xilio Development, Inc. | Masked cytokine polypeptides |
| CN113490688A (zh) | 2018-12-26 | 2021-10-08 | 希望之城公司 | 可活化的被掩蔽的抗ctla4结合蛋白质 |
| EP3957325A4 (en) | 2019-04-19 | 2023-01-04 | Chugai Seiyaku Kabushiki Kaisha | CHEMERA RECEPTOR RECOGNIZING AN ANTIBODY MODIFICATION SITE |
| KR20220023988A (ko) | 2019-05-14 | 2022-03-03 | 웨어울프 세라퓨틱스, 인크. | 분리 모이어티 및 이의 사용 방법 |
| CN114245802B (zh) | 2019-06-20 | 2024-10-15 | 石药集团巨石生物制药有限公司 | 修饰的il-2蛋白、peg偶联物及其用途 |
| EP3998083A4 (en) | 2019-07-12 | 2023-08-23 | Chugai Seiyaku Kabushiki Kaisha | ANTI-MUTATION TYPE FGFR3 ANTIBODY AND USE THEREOF |
| CA3155981A1 (en) | 2019-11-14 | 2021-05-20 | William Winston | Activatable cytokine polypeptides and methods of use thereof |
| TW202204601A (zh) | 2020-04-15 | 2022-02-01 | 美商建南德克公司 | 銅損失減緩 |
| EP4143225A4 (en) | 2020-04-27 | 2024-05-15 | The Regents of the University of California | ISOFORM-INDEPENDENT ANTIBODIES AGAINST LIPOPROTEIN(A) |
| WO2022140797A1 (en) | 2020-12-23 | 2022-06-30 | Immunowake Inc. | Immunocytokines and uses thereof |
| CA3209364A1 (en) | 2021-03-01 | 2022-09-09 | Jennifer O'neil | Combination of masked ctla4 and pd1/pdl1 antibodies for treating cancer |
| EP4301467A1 (en) | 2021-03-01 | 2024-01-10 | Xilio Development, Inc. | Combination of ctla4 and pd1/pdl1 antibodies for treating cancer |
| WO2022192898A2 (en) | 2021-03-10 | 2022-09-15 | Immunowake Inc. | Immunomodulatory molecules and uses thereof |
| US20240150466A1 (en) | 2021-03-25 | 2024-05-09 | Dynamicure Biotechnology Llc | Anti-igfbp7 constructs and uses thereof |
| EP4433080A1 (en) | 2021-11-18 | 2024-09-25 | Matrivax, Inc. | Immunogenic fusion protein compositions and methods of use thereof |
| WO2023131901A1 (en) | 2022-01-07 | 2023-07-13 | Johnson & Johnson Enterprise Innovation Inc. | Materials and methods of il-1beta binding proteins |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL86455A0 (en) * | 1987-06-01 | 1988-11-15 | Takeda Chemical Industries Ltd | Polypeptide and production thereof |
| JPH0638771A (ja) * | 1990-10-31 | 1994-02-15 | Tonen Corp | ヒトプロテインジスルフィドイソメラーゼ遺伝子の発現方法および該遺伝子との共発現によるポリペプチドの製造方法 |
| US5292646A (en) * | 1991-02-06 | 1994-03-08 | Genetics Institute, Inc. | Peptide and protein fusions to thioredoxin and thioredoxin-like molecules |
| US5270181A (en) * | 1991-02-06 | 1993-12-14 | Genetics Institute, Inc. | Peptide and protein fusions to thioredoxin and thioredoxin-like molecules |
| EP0509841A3 (en) * | 1991-04-18 | 1993-08-18 | Tonen Corporation | Co-expression system of protein disulfide isomerase gene and useful polypeptide gene and process for producing the polypeptide using its system |
| DE4113750A1 (de) * | 1991-04-26 | 1992-10-29 | Boehringer Mannheim Gmbh | Verbesserung der renaturierung bei der sekretion von disulfidverbrueckten proteinen |
| US6291205B1 (en) * | 1992-06-12 | 2001-09-18 | Merck & Co., Inc. | Method of increasing production of disulfide bonded recombinant proteins by saccharomyces cerevisiae |
| DE69329202T2 (de) * | 1992-10-02 | 2001-03-29 | Research Corp. Technologies, Inc. | Methoden der erhöhung der sekretion von überexpremierten proteinen |
-
1994
- 1994-11-03 US US08/333,912 patent/US5639635A/en not_active Expired - Lifetime
-
1995
- 1995-10-11 CA CA002203373A patent/CA2203373C/en not_active Expired - Lifetime
- 1995-10-11 WO PCT/US1995/014623 patent/WO1996014422A1/en active IP Right Grant
- 1995-10-11 ES ES95939877T patent/ES2259440T3/es not_active Expired - Lifetime
- 1995-10-11 MX MX9703012A patent/MX9703012A/es unknown
- 1995-10-11 JP JP51488896A patent/JP3749257B2/ja not_active Expired - Lifetime
- 1995-10-11 DK DK95939877T patent/DK0786009T3/da active
- 1995-10-11 DE DE69534822T patent/DE69534822T2/de not_active Expired - Lifetime
- 1995-10-11 AT AT95939877T patent/ATE318917T1/de active
- 1995-10-11 EP EP95939877A patent/EP0786009B1/en not_active Expired - Lifetime
- 1995-10-31 IL IL11583495A patent/IL115834A/en not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| ES2259440T3 (es) | 2006-10-01 |
| DE69534822T2 (de) | 2006-10-19 |
| WO1996014422A1 (en) | 1996-05-17 |
| CA2203373A1 (en) | 1996-05-17 |
| JPH10508203A (ja) | 1998-08-18 |
| JP3749257B2 (ja) | 2006-02-22 |
| DK0786009T3 (da) | 2006-07-03 |
| EP0786009A1 (en) | 1997-07-30 |
| CA2203373C (en) | 2007-08-28 |
| US5639635A (en) | 1997-06-17 |
| MX9703012A (es) | 1997-07-31 |
| EP0786009B1 (en) | 2006-03-01 |
| DE69534822D1 (de) | 2006-04-27 |
| ATE318917T1 (de) | 2006-03-15 |
| IL115834A0 (en) | 1996-01-19 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5639635A (en) | Process for bacterial production of polypeptides | |
| US5789199A (en) | Process for bacterial production of polypeptides | |
| AU671512B2 (en) | Method of controlling polypeptide production in bacteria | |
| US7229787B2 (en) | Method of N-terminal cleavage using an aminopeptidase | |
| AU2002326884A1 (en) | Aminopeptidase | |
| JP4510059B2 (ja) | ポリペプチドの製造方法 | |
| US8183029B2 (en) | Replicable expression vector for bacterial expression of a mammalian polypeptide | |
| US7829687B2 (en) | Artificial disulfide isomerases and uses thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FF | Patent granted | ||
| KB | Patent renewed | ||
| KB | Patent renewed | ||
| KB | Patent renewed | ||
| KB | Patent renewed | ||
| EXP | Patent expired |