NO893452L - Rekombinant naturlig dreper-celleaktivator. - Google Patents

Rekombinant naturlig dreper-celleaktivator.

Info

Publication number: NO893452L
Authority: NO; Norway
Prior art keywords: nkaf; cdna; cells; amino acid; plasmid
Prior art date: 1988-08-31

Application number

NO89893452A

Other languages

English (en)

Norwegian (no)

Other versions

NO893452D0 (no

Inventor

Kentaro Yoshimatsu

Yukio Ohya

Yasushi Shikata

Isao Tanaka

Yoshikazu Hasegawa

Toshio Seto

Toshiaki Osawa

Original Assignee

Eisai Co Ltd

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1988-08-31

Filing date

1989-08-29

Publication date

1990-03-01

1989-08-29 Application filed by Eisai Co Ltd filed Critical Eisai Co Ltd

1989-08-29 Publication of NO893452D0 publication Critical patent/NO893452D0/no

1990-03-01 Publication of NO893452L publication Critical patent/NO893452L/no

Links

239000012190 activator Substances 0.000 title 1
239000002299 complementary DNA Substances 0.000 claims abstract description 52
210000000822 natural killer cell Anatomy 0.000 claims abstract description 24
125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 22
239000013612 plasmid Substances 0.000 claims abstract description 19
108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 16
230000003213 activating effect Effects 0.000 claims abstract description 14
239000002246 antineoplastic agent Substances 0.000 claims abstract description 5
108090000623 proteins and genes Proteins 0.000 claims description 11
230000000259 anti-tumor effect Effects 0.000 claims description 4
230000033228 biological regulation Effects 0.000 claims description 4
239000000825 pharmaceutical preparation Substances 0.000 claims description 2
239000003795 chemical substances by application Substances 0.000 claims 1
239000008194 pharmaceutical composition Substances 0.000 abstract 1
210000004027 cell Anatomy 0.000 description 47
230000000694 effects Effects 0.000 description 31
239000012634 fragment Substances 0.000 description 26
238000000034 method Methods 0.000 description 18
108020004999 messenger RNA Proteins 0.000 description 14
238000002360 preparation method Methods 0.000 description 14
239000000203 mixture Substances 0.000 description 13
108020004414 DNA Proteins 0.000 description 12
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
239000000872 buffer Substances 0.000 description 12
239000002609 medium Substances 0.000 description 12
235000000346 sugar Nutrition 0.000 description 11
239000013598 vector Substances 0.000 description 11
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 10
239000000047 product Substances 0.000 description 10
239000000523 sample Substances 0.000 description 10
210000001744 T-lymphocyte Anatomy 0.000 description 9
108010076504 Protein Sorting Signals Proteins 0.000 description 8
210000004408 hybridoma Anatomy 0.000 description 8
239000006228 supernatant Substances 0.000 description 8
206010028980 Neoplasm Diseases 0.000 description 7
239000012980 RPMI-1640 medium Substances 0.000 description 7
150000001413 amino acids Chemical class 0.000 description 7
238000004458 analytical method Methods 0.000 description 7
201000011510 cancer Diseases 0.000 description 7
241000588724 Escherichia coli Species 0.000 description 6
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 6
238000004519 manufacturing process Methods 0.000 description 6
239000011780 sodium chloride Substances 0.000 description 6
239000000243 solution Substances 0.000 description 6
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 5
241000699666 Mus <mouse, genus> Species 0.000 description 5
230000001580 bacterial effect Effects 0.000 description 5
238000010276 construction Methods 0.000 description 5
238000011534 incubation Methods 0.000 description 5
239000004033 plastic Substances 0.000 description 5
229920003023 plastic Polymers 0.000 description 5
102000004169 proteins and genes Human genes 0.000 description 5
238000004007 reversed phase HPLC Methods 0.000 description 5
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
108091032973 (ribonucleotides)n+m Proteins 0.000 description 4
102000011413 Chondroitinases and Chondroitin Lyases Human genes 0.000 description 4
108010023736 Chondroitinases and Chondroitin Lyases Proteins 0.000 description 4
102100039555 Galectin-7 Human genes 0.000 description 4
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 4
241001465754 Metazoa Species 0.000 description 4
108700026244 Open Reading Frames Proteins 0.000 description 4
230000001464 adherent effect Effects 0.000 description 4
239000007864 aqueous solution Substances 0.000 description 4
238000006243 chemical reaction Methods 0.000 description 4
239000003480 eluent Substances 0.000 description 4
239000013613 expression plasmid Substances 0.000 description 4
239000013604 expression vector Substances 0.000 description 4
239000000499 gel Substances 0.000 description 4
210000000265 leukocyte Anatomy 0.000 description 4
239000012528 membrane Substances 0.000 description 4
229960000485 methotrexate Drugs 0.000 description 4
102000004196 processed proteins & peptides Human genes 0.000 description 4
238000000746 purification Methods 0.000 description 4
239000000126 substance Substances 0.000 description 4
238000012360 testing method Methods 0.000 description 4
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
101000608772 Homo sapiens Galectin-7 Proteins 0.000 description 3
102000000588 Interleukin-2 Human genes 0.000 description 3
108010002350 Interleukin-2 Proteins 0.000 description 3
241000699670 Mus sp. Species 0.000 description 3
241000283973 Oryctolagus cuniculus Species 0.000 description 3
108010033276 Peptide Fragments Proteins 0.000 description 3
102000007079 Peptide Fragments Human genes 0.000 description 3
240000004808 Saccharomyces cerevisiae Species 0.000 description 3
101100221606 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) COS7 gene Proteins 0.000 description 3
229920002684 Sepharose Polymers 0.000 description 3
102000004142 Trypsin Human genes 0.000 description 3
108090000631 Trypsin Proteins 0.000 description 3
239000004480 active ingredient Substances 0.000 description 3
239000006285 cell suspension Substances 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
238000003776 cleavage reaction Methods 0.000 description 3
239000012228 culture supernatant Substances 0.000 description 3
230000007123 defense Effects 0.000 description 3
238000010353 genetic engineering Methods 0.000 description 3
239000011521 glass Substances 0.000 description 3
238000009396 hybridization Methods 0.000 description 3
230000001965 increasing effect Effects 0.000 description 3
238000002347 injection Methods 0.000 description 3
239000007924 injection Substances 0.000 description 3
230000014759 maintenance of location Effects 0.000 description 3
210000004379 membrane Anatomy 0.000 description 3
229920001184 polypeptide Polymers 0.000 description 3
230000007017 scission Effects 0.000 description 3
239000001488 sodium phosphate Substances 0.000 description 3
229910000162 sodium phosphate Inorganic materials 0.000 description 3
239000002904 solvent Substances 0.000 description 3
RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 3
239000012588 trypsin Substances 0.000 description 3
238000005406 washing Methods 0.000 description 3
229920000936 Agarose Polymers 0.000 description 2
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
101800001415 Bri23 peptide Proteins 0.000 description 2
101800000655 C-terminal peptide Proteins 0.000 description 2
102400000107 C-terminal peptide Human genes 0.000 description 2
210000001239 CD8-positive, alpha-beta cytotoxic T lymphocyte Anatomy 0.000 description 2
108091026890 Coding region Proteins 0.000 description 2
108020004635 Complementary DNA Proteins 0.000 description 2
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
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 2
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
102000008072 Lymphokines Human genes 0.000 description 2
108010074338 Lymphokines Proteins 0.000 description 2
108090000542 Lymphotoxin-alpha Proteins 0.000 description 2
102000004083 Lymphotoxin-alpha Human genes 0.000 description 2
206010027476 Metastases Diseases 0.000 description 2
NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 description 2
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 2
102000005348 Neuraminidase Human genes 0.000 description 2
108010006232 Neuraminidase Proteins 0.000 description 2
229930182473 O-glycoside Natural products 0.000 description 2
150000008444 O-glycosides Chemical class 0.000 description 2
229920005654 Sephadex Polymers 0.000 description 2
239000012507 Sephadex™ Substances 0.000 description 2
CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
108091081024 Start codon Proteins 0.000 description 2
QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
238000001042 affinity chromatography Methods 0.000 description 2
239000000427 antigen Substances 0.000 description 2
102000036639 antigens Human genes 0.000 description 2
108091007433 antigens Proteins 0.000 description 2
239000011324 bead Substances 0.000 description 2
230000015572 biosynthetic process Effects 0.000 description 2
239000001506 calcium phosphate Substances 0.000 description 2
229910000389 calcium phosphate Inorganic materials 0.000 description 2
235000011010 calcium phosphates Nutrition 0.000 description 2
239000003814 drug Substances 0.000 description 2
239000000839 emulsion Substances 0.000 description 2
238000000855 fermentation Methods 0.000 description 2
230000004151 fermentation Effects 0.000 description 2
229930182830 galactose Natural products 0.000 description 2
239000008103 glucose Substances 0.000 description 2
108010085617 glycopeptide alpha-N-acetylgalactosaminidase Proteins 0.000 description 2
239000001963 growth medium Substances 0.000 description 2
108010083213 heparitinsulfate lyase Proteins 0.000 description 2
230000002209 hydrophobic effect Effects 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
238000002955 isolation Methods 0.000 description 2
239000000463 material Substances 0.000 description 2
230000009401 metastasis Effects 0.000 description 2
238000002703 mutagenesis Methods 0.000 description 2
231100000350 mutagenesis Toxicity 0.000 description 2
239000002773 nucleotide Substances 0.000 description 2
125000003729 nucleotide group Chemical group 0.000 description 2
OIPPWFOQEKKFEE-UHFFFAOYSA-N orcinol Chemical compound CC1=CC(O)=CC(O)=C1 OIPPWFOQEKKFEE-UHFFFAOYSA-N 0.000 description 2
230000036961 partial effect Effects 0.000 description 2
210000003200 peritoneal cavity Anatomy 0.000 description 2
XOJVVFBFDXDTEG-UHFFFAOYSA-N pristane Chemical compound CC(C)CCCC(C)CCCC(C)CCCC(C)C XOJVVFBFDXDTEG-UHFFFAOYSA-N 0.000 description 2
230000008569 process Effects 0.000 description 2
239000011541 reaction mixture Substances 0.000 description 2
230000002829 reductive effect Effects 0.000 description 2
230000010076 replication Effects 0.000 description 2
238000011160 research Methods 0.000 description 2
108091008146 restriction endonucleases Proteins 0.000 description 2
230000003248 secreting effect Effects 0.000 description 2
230000028327 secretion Effects 0.000 description 2
238000012546 transfer Methods 0.000 description 2
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 2
210000004881 tumor cell Anatomy 0.000 description 2
241001515965 unidentified phage Species 0.000 description 2
238000001262 western blot Methods 0.000 description 2
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
GEYOCULIXLDCMW-UHFFFAOYSA-N 1,2-phenylenediamine Chemical compound NC1=CC=CC=C1N GEYOCULIXLDCMW-UHFFFAOYSA-N 0.000 description 1
FNEHAOQZWPHONV-UHFFFAOYSA-N 9h-carbazole;sulfuric acid Chemical compound OS(O)(=O)=O.C1=CC=C2C3=CC=CC=C3NC2=C1 FNEHAOQZWPHONV-UHFFFAOYSA-N 0.000 description 1
ATRRKUHOCOJYRX-UHFFFAOYSA-N Ammonium bicarbonate Chemical compound [NH4+].OC([O-])=O ATRRKUHOCOJYRX-UHFFFAOYSA-N 0.000 description 1
229910000013 Ammonium bicarbonate Inorganic materials 0.000 description 1
206010003445 Ascites Diseases 0.000 description 1
108090001008 Avidin Proteins 0.000 description 1
125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
208000005623 Carcinogenesis Diseases 0.000 description 1
229920002567 Chondroitin Polymers 0.000 description 1
108700010070 Codon Usage Proteins 0.000 description 1
WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
229920002271 DEAE-Sepharose Polymers 0.000 description 1
101150074155 DHFR gene Proteins 0.000 description 1
108020003215 DNA Probes Proteins 0.000 description 1
108010066072 DNA modification methylase EcoRI Proteins 0.000 description 1
239000003298 DNA probe Substances 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
239000006144 Dulbecco’s modiﬁed Eagle's medium Substances 0.000 description 1
229920001917 Ficoll Polymers 0.000 description 1
101000887163 Gallus gallus Gallinacin-4 Proteins 0.000 description 1
101000887166 Gallus gallus Gallinacin-7 Proteins 0.000 description 1
108090000288 Glycoproteins Proteins 0.000 description 1
102000003886 Glycoproteins Human genes 0.000 description 1
229920002683 Glycosaminoglycan Polymers 0.000 description 1
MMFKFJORZBJVNF-UWVGGRQHSA-N His-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CN=CN1 MMFKFJORZBJVNF-UWVGGRQHSA-N 0.000 description 1
102000014150 Interferons Human genes 0.000 description 1
108010050904 Interferons Proteins 0.000 description 1
XWOBNBRUDDUEEY-UWVGGRQHSA-N Leu-His Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CNC=N1 XWOBNBRUDDUEEY-UWVGGRQHSA-N 0.000 description 1
WHXSMMKQMYFTQS-UHFFFAOYSA-N Lithium Chemical compound [Li] WHXSMMKQMYFTQS-UHFFFAOYSA-N 0.000 description 1
102000009073 Macrophage Migration-Inhibitory Factors Human genes 0.000 description 1
108010048043 Macrophage Migration-Inhibitory Factors Proteins 0.000 description 1
125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
239000007832 Na2SO4 Substances 0.000 description 1
239000000020 Nitrocellulose Substances 0.000 description 1
BELBBZDIHDAJOR-UHFFFAOYSA-N Phenolsulfonephthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2S(=O)(=O)O1 BELBBZDIHDAJOR-UHFFFAOYSA-N 0.000 description 1
102000045595 Phosphoprotein Phosphatases Human genes 0.000 description 1
108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 1
206010035226 Plasma cell myeloma Diseases 0.000 description 1
239000002202 Polyethylene glycol Substances 0.000 description 1
108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
108091034057 RNA (poly(A)) Proteins 0.000 description 1
PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
229930006000 Sucrose Natural products 0.000 description 1
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 1
239000007983 Tris buffer Substances 0.000 description 1
208000036142 Viral infection Diseases 0.000 description 1
241000700605 Viruses Species 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
239000002253 acid Substances 0.000 description 1
239000013543 active substance Substances 0.000 description 1
239000000853 adhesive Substances 0.000 description 1
230000001070 adhesive effect Effects 0.000 description 1
239000002671 adjuvant Substances 0.000 description 1
238000000246 agarose gel electrophoresis Methods 0.000 description 1
230000002776 aggregation Effects 0.000 description 1
238000004220 aggregation Methods 0.000 description 1
101150115889 al gene Proteins 0.000 description 1
125000000539 amino acid group Chemical group 0.000 description 1
238000003277 amino acid sequence analysis Methods 0.000 description 1
235000012538 ammonium bicarbonate Nutrition 0.000 description 1
239000001099 ammonium carbonate Substances 0.000 description 1
210000004102 animal cell Anatomy 0.000 description 1
238000000376 autoradiography Methods 0.000 description 1
210000001185 bone marrow Anatomy 0.000 description 1
229940098773 bovine serum albumin Drugs 0.000 description 1
238000010805 cDNA synthesis kit Methods 0.000 description 1
239000001110 calcium chloride Substances 0.000 description 1
229910001628 calcium chloride Inorganic materials 0.000 description 1
244000309466 calf Species 0.000 description 1
238000011088 calibration curve Methods 0.000 description 1
230000036952 cancer formation Effects 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
229910052799 carbon Inorganic materials 0.000 description 1
231100000504 carcinogenesis Toxicity 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
239000001913 cellulose Substances 0.000 description 1
229920002678 cellulose Polymers 0.000 description 1
230000008859 change Effects 0.000 description 1
210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
238000010367 cloning Methods 0.000 description 1
238000004440 column chromatography Methods 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
238000013329 compounding Methods 0.000 description 1
ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
230000001472 cytotoxic effect Effects 0.000 description 1
230000001066 destructive effect Effects 0.000 description 1
230000029087 digestion Effects 0.000 description 1
239000012470 diluted sample Substances 0.000 description 1
238000004090 dissolution Methods 0.000 description 1
229940079593 drug Drugs 0.000 description 1
238000001035 drying Methods 0.000 description 1
238000004520 electroporation Methods 0.000 description 1
238000010828 elution Methods 0.000 description 1
230000002708 enhancing effect Effects 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
239000012894 fetal calf serum Substances 0.000 description 1
239000000945 filler Substances 0.000 description 1
239000000706 filtrate Substances 0.000 description 1
239000012530 fluid Substances 0.000 description 1
238000005194 fractionation Methods 0.000 description 1
238000001641 gel filtration chromatography Methods 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
239000003365 glass fiber Substances 0.000 description 1
125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
229960000789 guanidine hydrochloride Drugs 0.000 description 1
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
230000011132 hemopoiesis Effects 0.000 description 1
238000004128 high performance liquid chromatography Methods 0.000 description 1
108010025306 histidylleucine Proteins 0.000 description 1
210000005104 human peripheral blood lymphocyte Anatomy 0.000 description 1
230000007062 hydrolysis Effects 0.000 description 1
238000006460 hydrolysis reaction Methods 0.000 description 1
230000003053 immunization Effects 0.000 description 1
230000006698 induction Effects 0.000 description 1
230000000977 initiatory effect Effects 0.000 description 1
229940079322 interferon Drugs 0.000 description 1
239000013067 intermediate product Substances 0.000 description 1
238000010253 intravenous injection Methods 0.000 description 1
238000011835 investigation Methods 0.000 description 1
238000004255 ion exchange chromatography Methods 0.000 description 1
108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
230000002147 killing effect Effects 0.000 description 1
229910052744 lithium Inorganic materials 0.000 description 1
210000004698 lymphocyte Anatomy 0.000 description 1
230000002934 lysing effect Effects 0.000 description 1
210000002540 macrophage Anatomy 0.000 description 1
UEGPKNKPLBYCNK-UHFFFAOYSA-L magnesium acetate Chemical compound [Mg+2].CC([O-])=O.CC([O-])=O UEGPKNKPLBYCNK-UHFFFAOYSA-L 0.000 description 1
210000004962 mammalian cell Anatomy 0.000 description 1
239000003226 mitogen Substances 0.000 description 1
229960004857 mitomycin Drugs 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
230000035772 mutation Effects 0.000 description 1
230000000869 mutational effect Effects 0.000 description 1
201000000050 myeloid neoplasm Diseases 0.000 description 1
229930014626 natural product Natural products 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
229920001220 nitrocellulos Polymers 0.000 description 1
108020004707 nucleic acids Proteins 0.000 description 1
102000039446 nucleic acids Human genes 0.000 description 1
150000007523 nucleic acids Chemical class 0.000 description 1
239000002245 particle Substances 0.000 description 1
239000008188 pellet Substances 0.000 description 1
238000012510 peptide mapping method Methods 0.000 description 1
102000013415 peroxidase activity proteins Human genes 0.000 description 1
108040007629 peroxidase activity proteins Proteins 0.000 description 1
229960003531 phenolsulfonphthalein Drugs 0.000 description 1
239000013600 plasmid vector Substances 0.000 description 1
229920001223 polyethylene glycol Polymers 0.000 description 1
229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
239000001267 polyvinylpyrrolidone Substances 0.000 description 1
235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
239000012521 purified sample Substances 0.000 description 1
230000036647 reaction Effects 0.000 description 1
230000006798 recombination Effects 0.000 description 1
238000005070 sampling Methods 0.000 description 1
238000012216 screening Methods 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000012163 sequencing technique Methods 0.000 description 1
238000013207 serial dilution Methods 0.000 description 1
238000007493 shaping process Methods 0.000 description 1
235000017281 sodium acetate Nutrition 0.000 description 1
229910000029 sodium carbonate Inorganic materials 0.000 description 1
239000001509 sodium citrate Substances 0.000 description 1
NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
229910052938 sodium sulfate Inorganic materials 0.000 description 1
235000011152 sodium sulphate Nutrition 0.000 description 1
238000000527 sonication Methods 0.000 description 1
241000894007 species Species 0.000 description 1
210000000952 spleen Anatomy 0.000 description 1
210000004989 spleen cell Anatomy 0.000 description 1
230000002269 spontaneous effect Effects 0.000 description 1
238000003756 stirring Methods 0.000 description 1
238000012916 structural analysis Methods 0.000 description 1
239000000758 substrate Substances 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
150000008163 sugars Chemical class 0.000 description 1
239000012134 supernatant fraction Substances 0.000 description 1
230000001629 suppression Effects 0.000 description 1
239000000725 suspension Substances 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
230000001225 therapeutic effect Effects 0.000 description 1
210000001541 thymus gland Anatomy 0.000 description 1
238000001890 transfection Methods 0.000 description 1
230000009466 transformation Effects 0.000 description 1
230000001052 transient effect Effects 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
238000000108 ultra-filtration Methods 0.000 description 1
238000011144 upstream manufacturing Methods 0.000 description 1
210000003462 vein Anatomy 0.000 description 1
230000009385 viral infection Effects 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 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
- 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
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/82—Proteins from microorganisms
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/12—Growth hormone, growth factor other than t-cell or b-cell growth factor, and growth hormone releasing factor; related peptides

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Genetics & Genomics (AREA)
Zoology (AREA)
Engineering & Computer Science (AREA)
Molecular Biology (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
Biophysics (AREA)
Gastroenterology & Hepatology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Medicinal Chemistry (AREA)
Toxicology (AREA)
Bioinformatics & Cheminformatics (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
General Engineering & Computer Science (AREA)
Wood Science & Technology (AREA)
Physics & Mathematics (AREA)
Microbiology (AREA)
Plant Pathology (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Peptides Or Proteins (AREA)
Agricultural Chemicals And Associated Chemicals (AREA)
Beans For Foods Or Fodder (AREA)
Meat, Egg Or Seafood Products (AREA)

NO89893452A 1988-08-31 1989-08-29 Rekombinant naturlig dreper-celleaktivator. NO893452L (no)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP21759988		1988-08-31

Publications (2)

Publication Number	Publication Date
NO893452D0 NO893452D0 (no)	1989-08-29
NO893452L true NO893452L (no)	1990-03-01

Family

ID=16706821

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO89893452A NO893452L (no)	1988-08-31	1989-08-29	Rekombinant naturlig dreper-celleaktivator.

Country Status (10)

Country	Link
US (2)	US5185431A (fr)
EP (1)	EP0357067B1 (fr)
KR (1)	KR900003371A (fr)
AT (1)	ATE118037T1 (fr)
AU (1)	AU4009789A (fr)
CA (1)	CA1335360C (fr)
DE (1)	DE68920931T2 (fr)
DK (1)	DK424989A (fr)
FI (1)	FI893833A7 (fr)
NO (1)	NO893452L (fr)

Families Citing this family (17)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5457038A (en) *	1988-11-10	1995-10-10	Genetics Institute, Inc.	Natural killer stimulatory factor
US5811523A (en)	1988-11-10	1998-09-22	Trinchieri; Giorgio	Antibodies to natural killer stimulatory factor
ATE140483T1 (de) *	1988-11-10	1996-08-15	Genetics Inst	Natürlicher killerzellen-stimulationsfaktor
US6683046B1 (en)	1989-12-22	2004-01-27	Hoffmann-La Roche Inc.	Purification and characterization of cytotoxic lymphocyte maturation factor and monoclonal antibodies thereto
JP3479539B2 (ja)	1992-04-10	2003-12-15	エーザイ株式会社	ヒトアンチトロンビンｉｉｉ変異体
AU2818695A (en) *	1995-06-06	1996-12-24	Human Genome Sciences, Inc.	Natural killer cell enhancing factor c
US6255079B1 (en)	1995-06-06	2001-07-03	Human Genome Sciences, Inc.	Polynucleotides encoding natural killer cell enhancing factor C
WO1996040947A1 (fr) *	1995-06-07	1996-12-19	Washington University	Systeme bacterien recombine a viabilite limitee par l'environnement
EP0937147A1 (fr) *	1996-04-03	1999-08-25	Human Genome Sciences, Inc.	Facteur ii d'activation de cellules tueuses naturelles chez l'homme
US6448044B2 (en)	1996-04-03	2002-09-10	Human Genome Sciences, Inc.	DNA encoding human natural killer cell activating factor II
US7026456B1 (en)	1998-01-23	2006-04-11	Hoffman-La Roche, Inc.	Antibodies against human IL-12
EP1930438A1 (fr) *	2006-12-07	2008-06-11	Academisch Medisch Centrum bij de Universiteit van Amsterdam	Facteur de transcription pour l'activation de cellules tueuses, la différentiation et ses usages
US9616114B1 (en)	2014-09-18	2017-04-11	David Gordon Bermudes	Modified bacteria having improved pharmacokinetics and tumor colonization enhancing antitumor activity
US10676723B2 (en)	2015-05-11	2020-06-09	David Gordon Bermudes	Chimeric protein toxins for expression by therapeutic bacteria
US11129906B1 (en)	2016-12-07	2021-09-28	David Gordon Bermudes	Chimeric protein toxins for expression by therapeutic bacteria
US11180535B1 (en)	2016-12-07	2021-11-23	David Gordon Bermudes	Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria
CN114736268B (zh) *	2022-03-01	2024-09-27	吉林农业大学	一种提高活性肽ace抑制率的修饰方法、ace抑制肽及其应用

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS58110548A (ja) *	1981-12-24	1983-07-01	Asahi Chem Ind Co Ltd	新規な生理活性ペプチド
JPS6197224A (ja) *	1984-10-19	1986-05-15	Eisai Co Ltd	新規なリンホカイン

1989
- 1989-08-11 US US07/392,841 patent/US5185431A/en not_active Expired - Fee Related
- 1989-08-15 FI FI893833A patent/FI893833A7/fi not_active Application Discontinuation
- 1989-08-21 AU AU40097/89A patent/AU4009789A/en not_active Abandoned
- 1989-08-24 CA CA000609327A patent/CA1335360C/fr not_active Expired - Fee Related
- 1989-08-29 DK DK424989A patent/DK424989A/da not_active Application Discontinuation
- 1989-08-29 NO NO89893452A patent/NO893452L/no unknown
- 1989-08-31 KR KR1019890012546A patent/KR900003371A/ko not_active Ceased
- 1989-08-31 AT AT89116105T patent/ATE118037T1/de not_active IP Right Cessation
- 1989-08-31 EP EP89116105A patent/EP0357067B1/fr not_active Expired - Lifetime
- 1989-08-31 DE DE68920931T patent/DE68920931T2/de not_active Expired - Fee Related
1992
- 1992-10-15 US US07/961,521 patent/US5316933A/en not_active Expired - Fee Related

Also Published As

Publication number	Publication date
CA1335360C (fr)	1995-04-25
US5316933A (en)	1994-05-31
EP0357067A2 (fr)	1990-03-07
DE68920931T2 (de)	1995-07-06
DE68920931D1 (de)	1995-03-16
US5185431A (en)	1993-02-09
EP0357067A3 (fr)	1991-08-21
FI893833A0 (fi)	1989-08-15
DK424989A (da)	1990-03-01
FI893833A7 (fi)	1990-03-01
EP0357067B1 (fr)	1995-02-01
AU4009789A (en)	1990-03-08
KR900003371A (ko)	1990-03-26
NO893452D0 (no)	1989-08-29
DK424989D0 (da)	1989-08-29
ATE118037T1 (de)	1995-02-15

Publication	Publication Date	Title
DK175583B1 (da)	2004-12-13	DNA-sekvenser kodende for interleukin-4-receptorer, RNA komplementært til disse, rekombinant ekspressionsvektor omfattende disse DNA-sekvenser, værtscelle transfekteret med denne vektor, fremgangsmåde til fremstilling af.
US6362325B1 (en)	2002-03-26	Murine 4-1BB gene
JP3542127B2 (ja)	2004-07-14	ヒトインターフェロン―β２／インターロイキン―６受容体
JP2804237B2 (ja)	1998-09-24	組換えリンホトキシンをコードするｄｎａ
JP2644794B2 (ja)	1997-08-25	新規な型のコロニー刺激因子―１
IE883523L (en)	1989-05-25	Interleukin-1 Receptors
NO174473B (no)	1994-01-31	Fremgangsmaate og ekspresjonsvektor til fremstilling av human TNF
JP2749838B2 (ja)	1998-05-13	インターロイキン−７
EP0357067B1 (fr)	1995-02-01	Activateur recombinant pour une cellule "killer" naturelle
JPH06505631A (ja)	1994-06-30	巨核球刺激因子
JPH09506506A (ja)	1997-06-30	ラミニンのＢ１ｋ鎖及び利用方法
US6709837B1 (en)	2004-03-23	Polypeptide and production thereof
JPH01501361A (ja)	1989-05-18	新しいｔ細胞サプレッサー因子の生産およびその用途
WO2011147320A1 (fr)	2011-12-01	Antagoniste du facteur d'activation des lymphocytes b et son procédé de préparation et son utilisation
EP0628055A1 (fr)	1994-12-14	Facteur cytotoxique tumoral modifie
US5728548A (en)	1998-03-17	Retinoid receptor-1 (RR1) and DNA encoding RR1
EP0702725B1 (fr)	2006-07-05	Procede de production recombinante de polypeptides a activite biologique
US5786168A (en)	1998-07-28	Method for recombinant production of antigen non-specific glycosylation inhibiting factor (GIF)
US6893844B1 (en)	2005-05-17	DNA encoding a new human hepatoma derived growth factor and producing method thereof
US5459049A (en)	1995-10-17	Motilin-like polypeptide and use thereof
CN100443501C (zh)	2008-12-17	人骨髓基质细胞来源的线粒体转运蛋白分子及其编码序列和用途
US7361486B2 (en)	2008-04-22	Polynucleotide, vector, host cell and method for producing human hepatoma-derived growth factor 5 polypeptide
JP3534434B2 (ja)	2004-06-07	トロンボモジュリン類発現用シグナルペプチド
US20060063923A1 (en)	2006-03-23	4-1BB peptides and methods for use
DK172382B1 (da)	1998-05-04	Rekombinante lymphotoxinderivater