ZA200102718B - Phospholipid derivatives of non-steroidal anti-inflammatory drugs. - Google Patents
Phospholipid derivatives of non-steroidal anti-inflammatory drugs. Download PDFInfo
- Publication number
- ZA200102718B ZA200102718B ZA200102718A ZA200102718A ZA200102718B ZA 200102718 B ZA200102718 B ZA 200102718B ZA 200102718 A ZA200102718 A ZA 200102718A ZA 200102718 A ZA200102718 A ZA 200102718A ZA 200102718 B ZA200102718 B ZA 200102718B
- Authority
- ZA
- South Africa
- Prior art keywords
- pek
- antibody
- seq
- group
- assay surface
- Prior art date
Links
- 229940021182 non-steroidal anti-inflammatory drug Drugs 0.000 title abstract 3
- 150000003904 phospholipids Chemical class 0.000 title abstract 2
- 238000000034 method Methods 0.000 claims abstract description 22
- 108090000623 proteins and genes Proteins 0.000 claims description 39
- 102000004169 proteins and genes Human genes 0.000 claims description 25
- 108091000080 Phosphotransferase Proteins 0.000 claims description 18
- 102000020233 phosphotransferase Human genes 0.000 claims description 18
- 238000003556 assay Methods 0.000 claims description 12
- 239000013598 vector Substances 0.000 claims description 11
- 230000003100 immobilizing effect Effects 0.000 claims description 10
- 150000007523 nucleic acids Chemical group 0.000 claims description 8
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 6
- 235000015097 nutrients Nutrition 0.000 claims description 5
- 239000000203 mixture Substances 0.000 claims description 4
- 108091033319 polynucleotide Proteins 0.000 claims description 4
- 102000040430 polynucleotide Human genes 0.000 claims description 4
- 239000002157 polynucleotide Substances 0.000 claims description 4
- 238000005406 washing Methods 0.000 claims description 4
- 102100038045 Eukaryotic translation initiation factor 2A Human genes 0.000 claims description 3
- 101710092068 Eukaryotic translation initiation factor 2A Proteins 0.000 claims description 3
- 238000004519 manufacturing process Methods 0.000 claims description 3
- 241000588724 Escherichia coli Species 0.000 claims description 2
- 108020004511 Recombinant DNA Proteins 0.000 claims description 2
- 239000013060 biological fluid Substances 0.000 claims 4
- 102100034285 Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A Human genes 0.000 claims 2
- 101710169586 Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A Proteins 0.000 claims 2
- 125000003275 alpha amino acid group Chemical group 0.000 claims 2
- 239000012472 biological sample Substances 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 238000000163 radioactive labelling Methods 0.000 claims 1
- 239000000523 sample Substances 0.000 claims 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 claims 1
- 230000015572 biosynthetic process Effects 0.000 abstract description 2
- 238000003786 synthesis reaction Methods 0.000 abstract description 2
- 150000001875 compounds Chemical class 0.000 abstract 3
- 208000037765 diseases and disorders Diseases 0.000 abstract 1
- 230000004968 inflammatory condition Effects 0.000 abstract 1
- 239000008194 pharmaceutical composition Substances 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 41
- 241000282414 Homo sapiens Species 0.000 description 16
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 11
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 11
- 239000000126 substance Substances 0.000 description 11
- 230000002163 immunogen Effects 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 239000002299 complementary DNA Substances 0.000 description 8
- 239000003623 enhancer Substances 0.000 description 8
- 102000008014 Eukaryotic Initiation Factor-2 Human genes 0.000 description 7
- 108010089791 Eukaryotic Initiation Factor-2 Proteins 0.000 description 7
- 241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 7
- 108010089429 PERK kinase Proteins 0.000 description 7
- 230000008878 coupling Effects 0.000 description 7
- 238000010168 coupling process Methods 0.000 description 7
- 238000005859 coupling reaction Methods 0.000 description 7
- 239000013604 expression vector Substances 0.000 description 7
- 230000035897 transcription Effects 0.000 description 7
- 238000013518 transcription Methods 0.000 description 7
- 108091026890 Coding region Proteins 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 6
- 241000699666 Mus <mouse, genus> Species 0.000 description 6
- 108700026244 Open Reading Frames Proteins 0.000 description 6
- 239000012634 fragment Substances 0.000 description 6
- 230000004927 fusion Effects 0.000 description 6
- 230000014616 translation Effects 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 206010035226 Plasma cell myeloma Diseases 0.000 description 5
- 241000700159 Rattus Species 0.000 description 5
- 150000001413 amino acids Chemical class 0.000 description 5
- 201000000050 myeloid neoplasm Diseases 0.000 description 5
- 108090000765 processed proteins & peptides Proteins 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 4
- 241000206602 Eukaryota Species 0.000 description 4
- 102100034170 Interferon-induced, double-stranded RNA-activated protein kinase Human genes 0.000 description 4
- 108091081024 Start codon Proteins 0.000 description 4
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Natural products O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 4
- 230000012010 growth Effects 0.000 description 4
- 210000004408 hybridoma Anatomy 0.000 description 4
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 4
- 210000003292 kidney cell Anatomy 0.000 description 4
- 230000026731 phosphorylation Effects 0.000 description 4
- 238000006366 phosphorylation reaction Methods 0.000 description 4
- 241000894007 species Species 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 3
- 229930193140 Neomycin Natural products 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 239000011324 bead Substances 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 150000004676 glycans Chemical class 0.000 description 3
- 230000001939 inductive effect Effects 0.000 description 3
- 230000000977 initiatory effect Effects 0.000 description 3
- 210000004962 mammalian cell Anatomy 0.000 description 3
- 229960004927 neomycin Drugs 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 229920001282 polysaccharide Polymers 0.000 description 3
- 239000005017 polysaccharide Substances 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 238000001243 protein synthesis Methods 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- OSJPPGNTCRNQQC-UWTATZPHSA-N 3-phospho-D-glyceric acid Chemical compound OC(=O)[C@H](O)COP(O)(O)=O OSJPPGNTCRNQQC-UWTATZPHSA-N 0.000 description 2
- -1 8V40 Proteins 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 2
- 241000282552 Chlorocebus aethiops Species 0.000 description 2
- 101150074155 DHFR gene Proteins 0.000 description 2
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 2
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 2
- 102000005731 Glucose-6-phosphate isomerase Human genes 0.000 description 2
- 108010070600 Glucose-6-phosphate isomerase Proteins 0.000 description 2
- 101000926525 Homo sapiens eIF-2-alpha kinase GCN2 Proteins 0.000 description 2
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 101150003725 TK gene Proteins 0.000 description 2
- 102000006601 Thymidine Kinase Human genes 0.000 description 2
- 108020004440 Thymidine kinase Proteins 0.000 description 2
- 208000036142 Viral infection Diseases 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 230000002411 adverse Effects 0.000 description 2
- 150000001299 aldehydes Chemical class 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
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 238000004440 column chromatography Methods 0.000 description 2
- 102100034175 eIF-2-alpha kinase GCN2 Human genes 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 2
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 239000003112 inhibitor Substances 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
- 238000002955 isolation Methods 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 2
- HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 2
- 229960000951 mycophenolic acid Drugs 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 229940104230 thymidine Drugs 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 230000009385 viral infection Effects 0.000 description 2
- DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 1
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- 102000013563 Acid Phosphatase Human genes 0.000 description 1
- 108010051457 Acid Phosphatase Proteins 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 101710187573 Alcohol dehydrogenase 2 Proteins 0.000 description 1
- 101710133776 Alcohol dehydrogenase class-3 Proteins 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 101100107610 Arabidopsis thaliana ABCF4 gene Proteins 0.000 description 1
- 238000011725 BALB/c mouse Methods 0.000 description 1
- 108700003860 Bacterial Genes Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 108091062157 Cis-regulatory element Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- 101100172226 Drosophila melanogaster emc gene Proteins 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108010042407 Endonucleases Proteins 0.000 description 1
- 102000004533 Endonucleases Human genes 0.000 description 1
- 102100030013 Endoribonuclease Human genes 0.000 description 1
- 101710199605 Endoribonuclease Proteins 0.000 description 1
- 241001522878 Escherichia coli B Species 0.000 description 1
- 241001646716 Escherichia coli K-12 Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 102000030595 Glucokinase Human genes 0.000 description 1
- 108010021582 Glucokinase Proteins 0.000 description 1
- 102000016285 Guanine Nucleotide Exchange Factors Human genes 0.000 description 1
- 108010067218 Guanine Nucleotide Exchange Factors Proteins 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102000005548 Hexokinase Human genes 0.000 description 1
- 108700040460 Hexokinases Proteins 0.000 description 1
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 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
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 102000003792 Metallothionein Human genes 0.000 description 1
- 108090000157 Metallothionein Proteins 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 101150097531 PEK gene Proteins 0.000 description 1
- 102000016387 Pancreatic elastase Human genes 0.000 description 1
- 108010067372 Pancreatic elastase Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108010044843 Peptide Initiation Factors Proteins 0.000 description 1
- 102000005877 Peptide Initiation Factors Human genes 0.000 description 1
- 102000001105 Phosphofructokinases Human genes 0.000 description 1
- 108010069341 Phosphofructokinases Proteins 0.000 description 1
- 102000012288 Phosphopyruvate Hydratase Human genes 0.000 description 1
- 108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 108010009341 Protein Serine-Threonine Kinases Proteins 0.000 description 1
- 102000009516 Protein Serine-Threonine Kinases Human genes 0.000 description 1
- 108010011939 Pyruvate Decarboxylase Proteins 0.000 description 1
- 102000013009 Pyruvate Kinase Human genes 0.000 description 1
- 108020005115 Pyruvate Kinase Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 108020005091 Replication Origin Proteins 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 101100068078 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GCN4 gene Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 101710113029 Serine/threonine-protein kinase Proteins 0.000 description 1
- 241000700584 Simplexvirus Species 0.000 description 1
- 108091036066 Three prime untranslated region Proteins 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 102000005924 Triose-Phosphate Isomerase Human genes 0.000 description 1
- 108700015934 Triose-phosphate isomerases Proteins 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
- 241000588902 Zymomonas mobilis Species 0.000 description 1
- 238000004115 adherent culture Methods 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000002032 cellular defenses Effects 0.000 description 1
- 230000019522 cellular metabolic process Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000003413 degradative effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- 108020001096 dihydrofolate reductase Proteins 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000009509 drug development Methods 0.000 description 1
- 238000007876 drug discovery Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 210000000267 erythroid cell Anatomy 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 210000004265 eukaryotic small ribosome subunit Anatomy 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012847 fine chemical Substances 0.000 description 1
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 125000002485 formyl group Chemical group [H]C(*)=O 0.000 description 1
- 229930182830 galactose Natural products 0.000 description 1
- 108060003196 globin Proteins 0.000 description 1
- 102000018146 globin Human genes 0.000 description 1
- 230000002414 glycolytic effect Effects 0.000 description 1
- 229940025294 hemin Drugs 0.000 description 1
- BTIJJDXEELBZFS-QDUVMHSLSA-K hemin Chemical compound CC1=C(CCC(O)=O)C(C=C2C(CCC(O)=O)=C(C)\C(N2[Fe](Cl)N23)=C\4)=N\C1=C/C2=C(C)C(C=C)=C3\C=C/1C(C)=C(C=C)C/4=N\1 BTIJJDXEELBZFS-QDUVMHSLSA-K 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 231100000844 hepatocellular carcinoma Toxicity 0.000 description 1
- 235000003642 hunger Nutrition 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000002169 hydrotherapy Methods 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 229910010272 inorganic material Inorganic materials 0.000 description 1
- 239000011147 inorganic material Substances 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 210000004153 islets of langerhan Anatomy 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 210000005229 liver cell Anatomy 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 230000009712 regulation of translation Effects 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 238000012827 research and development Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 210000001995 reticulocyte Anatomy 0.000 description 1
- 239000012266 salt solution Substances 0.000 description 1
- 238000013391 scatchard analysis Methods 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 210000000717 sertoli cell Anatomy 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 230000037351 starvation Effects 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 101150035767 trp gene Proteins 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07F—ACYCLIC, CARBOCYCLIC OR HETEROCYCLIC COMPOUNDS CONTAINING ELEMENTS OTHER THAN CARBON, HYDROGEN, HALOGEN, OXYGEN, NITROGEN, SULFUR, SELENIUM OR TELLURIUM
- C07F9/00—Compounds containing elements of Groups 5 or 15 of the Periodic Table
- C07F9/02—Phosphorus compounds
- C07F9/06—Phosphorus compounds without P—C bonds
- C07F9/08—Esters of oxyacids of phosphorus
- C07F9/09—Esters of phosphoric acids
- C07F9/10—Phosphatides, e.g. lecithin
- C07F9/106—Adducts, complexes, salts of phosphatides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/06—Antiasthmatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/06—Antimigraine agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/08—Antiepileptics; Anticonvulsants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/14—Drugs for disorders of the nervous system for treating abnormal movements, e.g. chorea, dyskinesia
- A61P25/16—Anti-Parkinson drugs
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/28—Drugs for disorders of the nervous system for treating neurodegenerative disorders of the central nervous system, e.g. nootropic agents, cognition enhancers, drugs for treating Alzheimer's disease or other forms of dementia
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07F—ACYCLIC, CARBOCYCLIC OR HETEROCYCLIC COMPOUNDS CONTAINING ELEMENTS OTHER THAN CARBON, HYDROGEN, HALOGEN, OXYGEN, NITROGEN, SULFUR, SELENIUM OR TELLURIUM
- C07F9/00—Compounds containing elements of Groups 5 or 15 of the Periodic Table
- C07F9/02—Phosphorus compounds
- C07F9/06—Phosphorus compounds without P—C bonds
- C07F9/08—Esters of oxyacids of phosphorus
- C07F9/09—Esters of phosphoric acids
- C07F9/10—Phosphatides, e.g. lecithin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07F—ACYCLIC, CARBOCYCLIC OR HETEROCYCLIC COMPOUNDS CONTAINING ELEMENTS OTHER THAN CARBON, HYDROGEN, HALOGEN, OXYGEN, NITROGEN, SULFUR, SELENIUM OR TELLURIUM
- C07F9/00—Compounds containing elements of Groups 5 or 15 of the Periodic Table
- C07F9/02—Phosphorus compounds
- C07F9/547—Heterocyclic compounds, e.g. containing phosphorus as a ring hetero atom
- C07F9/553—Heterocyclic compounds, e.g. containing phosphorus as a ring hetero atom having one nitrogen atom as the only ring hetero atom
- C07F9/572—Five-membered rings
- C07F9/5728—Five-membered rings condensed with carbocyclic rings or carbocyclic ring systems
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Neurology (AREA)
- Biomedical Technology (AREA)
- Neurosurgery (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Pain & Pain Management (AREA)
- Pulmonology (AREA)
- Rheumatology (AREA)
- Dermatology (AREA)
- Physical Education & Sports Medicine (AREA)
- Immunology (AREA)
- Psychiatry (AREA)
- Psychology (AREA)
- Hospice & Palliative Care (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicinal Preparation (AREA)
- Steroid Compounds (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
IL12714398A IL127143A0 (en) | 1998-11-19 | 1998-11-19 | Phospholipid terivatives of non-steroidal anti inflammatory drugs |
Publications (1)
Publication Number | Publication Date |
---|---|
ZA200102718B true ZA200102718B (en) | 2001-10-05 |
Family
ID=11072158
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ZA200102718A ZA200102718B (en) | 1998-11-19 | 2001-04-03 | Phospholipid derivatives of non-steroidal anti-inflammatory drugs. |
Country Status (11)
Country | Link |
---|---|
US (3) | US6730696B1 (de) |
EP (1) | EP1131326B1 (de) |
JP (1) | JP2002530410A (de) |
AT (1) | ATE239739T1 (de) |
AU (1) | AU766045B2 (de) |
CA (1) | CA2346869C (de) |
DE (1) | DE69907720T2 (de) |
IL (1) | IL127143A0 (de) |
NZ (1) | NZ510938A (de) |
WO (1) | WO2000031083A1 (de) |
ZA (1) | ZA200102718B (de) |
Families Citing this family (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
IL127143A0 (en) | 1998-11-19 | 1999-09-22 | Dpharm Ltd | Phospholipid terivatives of non-steroidal anti inflammatory drugs |
US7410956B2 (en) * | 2002-02-11 | 2008-08-12 | Vertex Pharmaceuticals Incorporated | Caspase inhibitor prodrugs |
US20070053984A1 (en) * | 2005-03-03 | 2007-03-08 | Monique Spann-Wade | Topical gels compositions |
DE102006019907A1 (de) * | 2006-04-28 | 2007-10-31 | Müller-Enoch, Dieter, Prof. Dr. | Verwendung von substituierten Glycerinderivaten zur Herstellung einer pharmazeutischen Zubereitung |
US20080317684A1 (en) * | 2006-09-06 | 2008-12-25 | Isw Group, Inc. | Topical Compositions |
MX2010004885A (es) * | 2007-10-30 | 2010-08-04 | Athera Biotechnologies Ab | Diagnostico y metodos terapeuticos y composiciones para enfermedades cardiovasculares. |
WO2012073245A1 (en) | 2010-12-02 | 2012-06-07 | Ben Gurion University Of The Negev Research And Development Authority | Conjugates of a phospholipid and a drug for the treatment of inflammatory bowel disease |
US20230285292A1 (en) * | 2020-06-23 | 2023-09-14 | The Trustees Of The University Of Pennsylvania | Compositions and methods of using a pla2-responsive drug delivery system |
Family Cites Families (13)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5223263A (en) | 1988-07-07 | 1993-06-29 | Vical, Inc. | Liponucleotide-containing liposomes |
US5352673A (en) * | 1989-08-29 | 1994-10-04 | Dennis Edward A | Prodrugs |
WO1991016920A1 (en) | 1990-05-07 | 1991-11-14 | Vical, Inc. | Lipid prodrugs of salicylate and nonsteroidal anti-inflammatory drugs |
US5563257A (en) * | 1990-08-20 | 1996-10-08 | Boehringer Mannheim Gmbh | Phospholipid derivatives of nucleosides |
US5543389A (en) | 1990-11-01 | 1996-08-06 | State Of Oregon, Acting By And Through The Oregon State Board Of Higher Education On Behalf Of The Oregon Health Sciences University, A Non Profit Organization | Covalent polar lipid-peptide conjugates for use in salves |
US5256641A (en) | 1990-11-01 | 1993-10-26 | State Of Oregon | Covalent polar lipid-peptide conjugates for immunological targeting |
US5149794A (en) | 1990-11-01 | 1992-09-22 | State Of Oregon | Covalent lipid-drug conjugates for drug targeting |
CA2112803A1 (en) | 1991-07-12 | 1993-01-21 | Karl Y. Hostetler | Antiviral liponucleosides: treatment of hepatitis b |
JPH07188280A (ja) * | 1993-12-28 | 1995-07-25 | L T T Kenkyusho:Kk | ホスファチジルエタノールアミン類結合生理活性物質およびその中間体 |
US5534499A (en) * | 1994-05-19 | 1996-07-09 | The University Of British Columbia | Lipophilic drug derivatives for use in liposomes |
ATE218872T1 (de) | 1995-01-27 | 2002-06-15 | Univ Texas | Verfahren zur erhöhung der therapeutischen wirkung von nsaids und dazu verwendbare zwitterionische phospholipidhaltige zusammensetungen |
JP3781877B2 (ja) * | 1997-10-03 | 2006-05-31 | 株式会社ムック | アスコルビン酸誘導体またはその塩、および医薬 |
IL127143A0 (en) * | 1998-11-19 | 1999-09-22 | Dpharm Ltd | Phospholipid terivatives of non-steroidal anti inflammatory drugs |
-
1998
- 1998-11-19 IL IL12714398A patent/IL127143A0/xx unknown
-
1999
- 1999-11-18 EP EP99956297A patent/EP1131326B1/de not_active Expired - Lifetime
- 1999-11-18 NZ NZ510938A patent/NZ510938A/xx not_active IP Right Cessation
- 1999-11-18 AU AU12928/00A patent/AU766045B2/en not_active Ceased
- 1999-11-18 DE DE69907720T patent/DE69907720T2/de not_active Expired - Lifetime
- 1999-11-18 WO PCT/IL1999/000623 patent/WO2000031083A1/en active IP Right Grant
- 1999-11-18 AT AT99956297T patent/ATE239739T1/de not_active IP Right Cessation
- 1999-11-18 US US09/856,009 patent/US6730696B1/en not_active Expired - Fee Related
- 1999-11-18 JP JP2000583911A patent/JP2002530410A/ja active Pending
- 1999-11-18 CA CA2346869A patent/CA2346869C/en not_active Expired - Fee Related
-
2001
- 2001-04-03 ZA ZA200102718A patent/ZA200102718B/en unknown
-
2004
- 2004-01-14 US US10/757,098 patent/US7173018B2/en not_active Expired - Lifetime
-
2006
- 2006-12-20 US US11/643,189 patent/US7417035B2/en not_active Expired - Fee Related
Also Published As
Publication number | Publication date |
---|---|
EP1131326A1 (de) | 2001-09-12 |
AU1292800A (en) | 2000-06-13 |
AU766045B2 (en) | 2003-10-09 |
ATE239739T1 (de) | 2003-05-15 |
US20070191310A1 (en) | 2007-08-16 |
DE69907720D1 (de) | 2003-06-12 |
US7173018B2 (en) | 2007-02-06 |
EP1131326B1 (de) | 2003-05-07 |
DE69907720T2 (de) | 2004-02-26 |
WO2000031083A1 (en) | 2000-06-02 |
JP2002530410A (ja) | 2002-09-17 |
US6730696B1 (en) | 2004-05-04 |
US20040147485A1 (en) | 2004-07-29 |
IL127143A0 (en) | 1999-09-22 |
EP1131326A4 (de) | 2002-03-27 |
NZ510938A (en) | 2002-11-26 |
CA2346869A1 (en) | 2000-06-02 |
US7417035B2 (en) | 2008-08-26 |
CA2346869C (en) | 2010-03-23 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CN102791726B (zh) | 纯化免疫球蛋白溶液的方法 | |
JP2592063B2 (ja) | リガンド、そのアンタゴニストまたはアゴニストの効率的な測定のためのハイブリツドリセプター | |
US7807791B2 (en) | Antibodies immunoreactive with mutant 5-enolpyruvlshikimate-3-phosphate synthase | |
JP6507522B2 (ja) | 改良Fc結合性タンパク質、当該タンパク質の製造方法および当該タンパク質を用いた抗体吸着剤 | |
EP2646606B1 (de) | Oberflächen-verankertes fc-beute-antikörperanzeigesystem | |
US10611817B2 (en) | Fc-binding protein, method for producing said protein, and antibody adsorbent using said protein, and methods for purifying and identifying antibody using said adsorbent | |
CN101074264A (zh) | 一种重组抗ctla4单克隆抗体及其制备方法和用途 | |
ZA200102718B (en) | Phospholipid derivatives of non-steroidal anti-inflammatory drugs. | |
WO2009107682A1 (ja) | ヒト型Fcレセプターをコードするポリヌクレオチド、およびそれを利用したヒト型Fcレセプターの製造方法 | |
JP2013510574A (ja) | チャイニーズハムスターからのグリコシルトランスフェラーゼおよび関連方法 | |
CN113402606B (zh) | 一种中性粒细胞明胶酶相关脂质运载蛋白检测试剂盒及其临床应用 | |
US11104721B2 (en) | Surface, anchored FC-bait antibody display system | |
AU751997B2 (en) | Pancreatic eukaryotic translation initiation factor-2alpha kinase | |
JP7009913B2 (ja) | アミノ酸置換したFc結合性タンパク質 | |
CN114230666B (zh) | 一种t7 rna聚合酶的单克隆抗体及其制备方法 | |
CN114262378B (zh) | 一种omt的单克隆抗体及其制备方法 | |
CN101074263A (zh) | 一种重组抗proteinA单克隆抗体及其制备方法和用途 | |
EP0619836A1 (de) | Methoden zur herstellung von gereinigten, löslichen pdgf-rezeptorfragmenten vom typ-a und typ-b aus mensch | |
CN113621059B (zh) | 一种β2-微球蛋白检测试剂盒及其临床应用 | |
JPH06501850A (ja) | チャイニーズハムスター卵巣細胞のレトロウイルス様粒子 | |
US20190300586A1 (en) | Artificial forisome bodies with seo-f fusion proteins, plant or yeast cells with vectors for encoding these proteins and vectors for encoding seo-f fusion proteins | |
Dulieu et al. | Production of monoclonal antibodies highly specific for virus-like particles from male-sterile Vicia faba. Development of a double sandwich ELISA allowing quantitative analysis of VLPs | |
JP2732960B2 (ja) | 組換えヒト・オステオカルシン | |
JP2011200203A (ja) | Fcレセプターの製造方法 | |
CN101074265A (zh) | 一种重组抗tnfr单克隆抗体及其制备方法和用途 |