NO311366B1 - Isolert nukleinsyremolekyl som koder for gp75, fremgangsmåte for å fremstille en aminosyresekvens fra samme, samt fremgangsmåtefor å fremstille vaksine - Google Patents
Isolert nukleinsyremolekyl som koder for gp75, fremgangsmåte for å fremstille en aminosyresekvens fra samme, samt fremgangsmåtefor å fremstille vaksine Download PDFInfo
- Publication number
- NO311366B1 NO311366B1 NO19923659A NO923659A NO311366B1 NO 311366 B1 NO311366 B1 NO 311366B1 NO 19923659 A NO19923659 A NO 19923659A NO 923659 A NO923659 A NO 923659A NO 311366 B1 NO311366 B1 NO 311366B1
- Authority
- NO
- Norway
- Prior art keywords
- fragment
- nucleic acid
- melanoma
- amino acid
- vaccine
- Prior art date
Links
- 125000003275 alpha amino acid group Chemical group 0.000 title claims abstract description 26
- 238000000034 method Methods 0.000 title claims abstract description 23
- 229960005486 vaccine Drugs 0.000 title claims abstract description 21
- 150000007523 nucleic acids Chemical class 0.000 title claims abstract description 20
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 18
- 108020004707 nucleic acids Proteins 0.000 title claims abstract description 17
- 102000039446 nucleic acids Human genes 0.000 title claims abstract description 17
- 239000002299 complementary DNA Substances 0.000 claims abstract description 67
- 239000012634 fragment Substances 0.000 claims abstract description 28
- 230000002708 enhancing effect Effects 0.000 claims abstract description 5
- 230000004936 stimulating effect Effects 0.000 claims abstract description 5
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 35
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 24
- 239000013604 expression vector Substances 0.000 claims description 16
- 239000002671 adjuvant Substances 0.000 claims description 13
- 229920001184 polypeptide Polymers 0.000 claims description 13
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 10
- 239000013612 plasmid Substances 0.000 claims description 10
- 241000588724 Escherichia coli Species 0.000 claims description 8
- 239000003937 drug carrier Substances 0.000 claims description 6
- 238000002156 mixing Methods 0.000 claims description 5
- 230000010076 replication Effects 0.000 claims description 5
- 239000013598 vector Substances 0.000 claims description 5
- 230000016784 immunoglobulin production Effects 0.000 claims description 3
- 241000700618 Vaccinia virus Species 0.000 claims description 2
- 206010028980 Neoplasm Diseases 0.000 abstract description 16
- 201000011510 cancer Diseases 0.000 abstract description 13
- 201000001441 melanoma Diseases 0.000 description 78
- 210000004027 cell Anatomy 0.000 description 64
- 108090000623 proteins and genes Proteins 0.000 description 63
- 102000004169 proteins and genes Human genes 0.000 description 54
- 239000000427 antigen Substances 0.000 description 42
- 102000036639 antigens Human genes 0.000 description 42
- 108091007433 antigens Proteins 0.000 description 42
- 230000000694 effects Effects 0.000 description 40
- 210000002752 melanocyte Anatomy 0.000 description 27
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 24
- 241000699666 Mus <mouse, genus> Species 0.000 description 21
- 108060008724 Tyrosinase Proteins 0.000 description 21
- 108091000117 Tyrosine 3-Monooxygenase Proteins 0.000 description 21
- 102000048218 Tyrosine 3-monooxygenases Human genes 0.000 description 21
- 239000000872 buffer Substances 0.000 description 21
- 102000003425 Tyrosinase Human genes 0.000 description 20
- 208000012641 Pigmentation disease Diseases 0.000 description 17
- 230000004069 differentiation Effects 0.000 description 17
- 230000019612 pigmentation Effects 0.000 description 17
- 239000007983 Tris buffer Substances 0.000 description 16
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 16
- 210000002966 serum Anatomy 0.000 description 16
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 16
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 15
- 108010062580 Concanavalin A Proteins 0.000 description 15
- 101000606090 Homo sapiens Tyrosinase Proteins 0.000 description 14
- 239000000499 gel Substances 0.000 description 14
- 239000012528 membrane Substances 0.000 description 14
- 101000773083 Homo sapiens 5,6-dihydroxyindole-2-carboxylic acid oxidase Proteins 0.000 description 13
- 238000004458 analytical method Methods 0.000 description 13
- 102100030310 5,6-dihydroxyindole-2-carboxylic acid oxidase Human genes 0.000 description 12
- 229920002684 Sepharose Polymers 0.000 description 12
- 150000001413 amino acids Chemical class 0.000 description 12
- 239000002773 nucleotide Substances 0.000 description 12
- 125000003729 nucleotide group Chemical group 0.000 description 12
- 239000011780 sodium chloride Substances 0.000 description 12
- 239000006228 supernatant Substances 0.000 description 12
- 108090000288 Glycoproteins Proteins 0.000 description 11
- 102000003886 Glycoproteins Human genes 0.000 description 11
- 238000010367 cloning Methods 0.000 description 11
- 239000000203 mixture Substances 0.000 description 11
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 11
- 238000002965 ELISA Methods 0.000 description 10
- 241000699670 Mus sp. Species 0.000 description 10
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
- 238000000746 purification Methods 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 8
- 108090000790 Enzymes Proteins 0.000 description 8
- XUMBMVFBXHLACL-UHFFFAOYSA-N Melanin Chemical compound O=C1C(=O)C(C2=CNC3=C(C(C(=O)C4=C32)=O)C)=C2C4=CNC2=C1C XUMBMVFBXHLACL-UHFFFAOYSA-N 0.000 description 8
- 238000005859 coupling reaction Methods 0.000 description 8
- 238000010828 elution Methods 0.000 description 8
- 238000002474 experimental method Methods 0.000 description 8
- 238000001114 immunoprecipitation Methods 0.000 description 8
- 238000002955 isolation Methods 0.000 description 8
- 101000608782 Mus musculus Tyrosinase Proteins 0.000 description 7
- 238000003556 assay Methods 0.000 description 7
- 230000006698 induction Effects 0.000 description 7
- 230000003834 intracellular effect Effects 0.000 description 7
- 210000002780 melanosome Anatomy 0.000 description 7
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 6
- 108020004414 DNA Proteins 0.000 description 6
- 239000002253 acid Substances 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- 210000002950 fibroblast Anatomy 0.000 description 6
- 239000012133 immunoprecipitate Substances 0.000 description 6
- 239000008188 pellet Substances 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 108010051815 Glutamyl endopeptidase Proteins 0.000 description 5
- 206010027480 Metastatic malignant melanoma Diseases 0.000 description 5
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 5
- 150000007513 acids Chemical class 0.000 description 5
- 230000008878 coupling Effects 0.000 description 5
- 238000010168 coupling process Methods 0.000 description 5
- 208000035250 cutaneous malignant susceptibility to 1 melanoma Diseases 0.000 description 5
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 5
- 230000029087 digestion Effects 0.000 description 5
- 239000000284 extract Substances 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 208000021039 metastatic melanoma Diseases 0.000 description 5
- 238000012163 sequencing technique Methods 0.000 description 5
- 229910052709 silver Inorganic materials 0.000 description 5
- 239000004332 silver Substances 0.000 description 5
- 241000701533 Escherichia virus T4 Species 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 4
- 241000221961 Neurospora crassa Species 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 4
- 239000003599 detergent Substances 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 4
- 230000001376 precipitating effect Effects 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 3
- 102000012750 Membrane Glycoproteins Human genes 0.000 description 3
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 239000001110 calcium chloride Substances 0.000 description 3
- 235000011148 calcium chloride Nutrition 0.000 description 3
- 229910001628 calcium chloride Inorganic materials 0.000 description 3
- 230000006957 competitive inhibition Effects 0.000 description 3
- 229960003964 deoxycholic acid Drugs 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 210000000987 immune system Anatomy 0.000 description 3
- 239000002751 oligonucleotide probe Substances 0.000 description 3
- 238000012510 peptide mapping method Methods 0.000 description 3
- 210000004694 pigment cell Anatomy 0.000 description 3
- 239000013600 plasmid vector Substances 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 230000017854 proteolysis Effects 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000000539 two dimensional gel electrophoresis Methods 0.000 description 3
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 3
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 208000002109 Argyria Diseases 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 108010054576 Deoxyribonuclease EcoRI 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
- 239000004471 Glycine Substances 0.000 description 2
- 208000003367 Hypopigmentation Diseases 0.000 description 2
- 229910021380 Manganese Chloride Inorganic materials 0.000 description 2
- GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 2
- 108010090054 Membrane Glycoproteins Proteins 0.000 description 2
- 101100154912 Mus musculus Tyrp1 gene Proteins 0.000 description 2
- 239000000020 Nitrocellulose Substances 0.000 description 2
- 239000002033 PVDF binder Substances 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 241000276498 Pollachius virens Species 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 101710172711 Structural protein Proteins 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 206010047642 Vitiligo Diseases 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 238000005349 anion exchange Methods 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 229940009976 deoxycholate Drugs 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
- 239000012149 elution buffer Substances 0.000 description 2
- 239000012894 fetal calf serum Substances 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 230000003425 hypopigmentation Effects 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000004807 localization Effects 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 229910001629 magnesium chloride Inorganic materials 0.000 description 2
- 239000011565 manganese chloride Substances 0.000 description 2
- 235000002867 manganese chloride Nutrition 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 229920001220 nitrocellulos Polymers 0.000 description 2
- 239000008177 pharmaceutical agent Substances 0.000 description 2
- QKFJKGMPGYROCL-UHFFFAOYSA-N phenyl isothiocyanate Chemical compound S=C=NC1=CC=CC=C1 QKFJKGMPGYROCL-UHFFFAOYSA-N 0.000 description 2
- -1 phenylthiocarbamyl amino Chemical class 0.000 description 2
- 239000000049 pigment Substances 0.000 description 2
- 238000004393 prognosis Methods 0.000 description 2
- KCXFHTAICRTXLI-UHFFFAOYSA-M propane-1-sulfonate Chemical compound CCCS([O-])(=O)=O KCXFHTAICRTXLI-UHFFFAOYSA-M 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 238000007790 scraping Methods 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 210000001768 subcellular fraction Anatomy 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 210000004881 tumor cell Anatomy 0.000 description 2
- HBOMLICNUCNMMY-KJFJCRTCSA-N 1-[(4s,5s)-4-azido-5-(hydroxymethyl)oxolan-2-yl]-5-methylpyrimidine-2,4-dione Chemical compound O=C1NC(=O)C(C)=CN1C1O[C@H](CO)[C@@H](N=[N+]=[N-])C1 HBOMLICNUCNMMY-KJFJCRTCSA-N 0.000 description 1
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- PMUNIMVZCACZBB-UHFFFAOYSA-N 2-hydroxyethylazanium;chloride Chemical compound Cl.NCCO PMUNIMVZCACZBB-UHFFFAOYSA-N 0.000 description 1
- 101710149506 28 kDa protein Proteins 0.000 description 1
- 108700000328 75kDa membrane Proteins 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-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
- 101000588395 Bacillus subtilis (strain 168) Beta-hexosaminidase Proteins 0.000 description 1
- 101001025146 Bartonella bacilliformis Cell division protein FtsZ Proteins 0.000 description 1
- 101000609456 Beet necrotic yellow vein virus (isolate Japan/S) Protein P26 Proteins 0.000 description 1
- 238000011740 C57BL/6 mouse Methods 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 101710137943 Complement control protein C3 Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 229920000209 Hexadimethrine bromide Polymers 0.000 description 1
- 241000282412 Homo Species 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
- 101710141452 Major surface glycoprotein G Proteins 0.000 description 1
- 206010064912 Malignant transformation Diseases 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 206010061309 Neoplasm progression Diseases 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 108091034057 RNA (poly(A)) Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 101000829189 Staphylococcus aureus Glutamyl endopeptidase Proteins 0.000 description 1
- 101000895926 Streptomyces plicatus Endo-beta-N-acetylglucosaminidase H Proteins 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
- 101710152003 Suppressor of silencing P0 Proteins 0.000 description 1
- 230000005867 T cell response Effects 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 101800003447 VP53 Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 238000005804 alkylation reaction Methods 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
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 230000002788 anti-peptide Effects 0.000 description 1
- 210000000612 antigen-presenting cell Anatomy 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- VDQQXEISLMTGAB-UHFFFAOYSA-N chloramine T Chemical compound [Na+].CC1=CC=C(S(=O)(=O)[N-]Cl)C=C1 VDQQXEISLMTGAB-UHFFFAOYSA-N 0.000 description 1
- YTRQFSDWAXHJCC-UHFFFAOYSA-N chloroform;phenol Chemical compound ClC(Cl)Cl.OC1=CC=CC=C1 YTRQFSDWAXHJCC-UHFFFAOYSA-N 0.000 description 1
- 238000011210 chromatographic step Methods 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 229960004397 cyclophosphamide Drugs 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- KXGVEGMKQFWNSR-UHFFFAOYSA-N deoxycholic acid Natural products C1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(O)=O)C)C1(C)C(O)C2 KXGVEGMKQFWNSR-UHFFFAOYSA-N 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- ZBCBWPMODOFKDW-UHFFFAOYSA-N diethanolamine Chemical compound OCCNCCO ZBCBWPMODOFKDW-UHFFFAOYSA-N 0.000 description 1
- KAKKHKRHCKCAGH-UHFFFAOYSA-L disodium;(4-nitrophenyl) phosphate;hexahydrate Chemical compound O.O.O.O.O.O.[Na+].[Na+].[O-][N+](=O)C1=CC=C(OP([O-])([O-])=O)C=C1 KAKKHKRHCKCAGH-UHFFFAOYSA-L 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000003370 dye binding method Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 239000006167 equilibration buffer Substances 0.000 description 1
- 239000003797 essential amino acid Substances 0.000 description 1
- 235000020776 essential amino acid Nutrition 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000012847 fine chemical Substances 0.000 description 1
- 238000010230 functional analysis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000003365 glass fiber Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 230000001894 hemadsorption Effects 0.000 description 1
- 230000004727 humoral immunity Effects 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000008073 immune recognition Effects 0.000 description 1
- 230000006058 immune tolerance Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000026045 iodination Effects 0.000 description 1
- 238000006192 iodination reaction Methods 0.000 description 1
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 230000036212 malign transformation Effects 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000035800 maturation Effects 0.000 description 1
- 230000008099 melanin synthesis Effects 0.000 description 1
- 230000000684 melanotic effect Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000017074 necrotic cell death Effects 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 238000002135 phase contrast microscopy Methods 0.000 description 1
- 229940117953 phenylisothiocyanate Drugs 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 239000011546 protein dye Substances 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 230000000306 recurrent effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 230000000405 serological effect Effects 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000003104 tissue culture media Substances 0.000 description 1
- 230000005751 tumor progression Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y110/00—Oxidoreductases acting on diphenols and related substances as donors (1.10)
- C12Y110/03—Oxidoreductases acting on diphenols and related substances as donors (1.10) with an oxygen as acceptor (1.10.3)
- C12Y110/03001—Catechol oxidase (1.10.3.1), i.e. tyrosinase
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- 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.)
- C12N9/0055—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10)
- C12N9/0057—Oxidoreductases (1.) acting on diphenols and related substances as donors (1.10) with oxygen as acceptor (1.10.3)
- C12N9/0059—Catechol oxidase (1.10.3.1), i.e. tyrosinase
-
- 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.)
- C12N9/0071—Oxidoreductases (1.) acting on paired donors with incorporation of molecular oxygen (1.14)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y114/00—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14)
- C12Y114/16—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14) with reduced pteridine as one donor, and incorporation of one atom of oxygen (1.14.16)
- C12Y114/16002—Tyrosine 3-monooxygenase (1.14.16.2)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y114/00—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14)
- C12Y114/18—Oxidoreductases acting on paired donors, with incorporation or reduction of molecular oxygen (1.14) with another compound as one donor, and incorporation of one atom of oxygen (1.14.18)
- C12Y114/18001—Tyrosinase (1.14.18.1)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US49743190A | 1990-03-22 | 1990-03-22 | |
| PCT/US1991/001942 WO1991014775A1 (en) | 1990-03-22 | 1991-03-22 | Gp75 as a tumor vaccine for melanoma |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO923659D0 NO923659D0 (no) | 1992-09-21 |
| NO923659L NO923659L (no) | 1992-11-06 |
| NO311366B1 true NO311366B1 (no) | 2001-11-19 |
Family
ID=23976841
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO19923659A NO311366B1 (no) | 1990-03-22 | 1992-09-21 | Isolert nukleinsyremolekyl som koder for gp75, fremgangsmåte for å fremstille en aminosyresekvens fra samme, samt fremgangsmåtefor å fremstille vaksine |
Country Status (21)
| Country | Link |
|---|---|
| US (2) | US6168946B1 (hu) |
| EP (2) | EP0522078B1 (hu) |
| JP (2) | JP3336006B2 (hu) |
| AT (1) | ATE187493T1 (hu) |
| AU (1) | AU660412B2 (hu) |
| CA (1) | CA2078773C (hu) |
| CZ (1) | CZ290278B6 (hu) |
| DE (1) | DE69131829T2 (hu) |
| DK (1) | DK0522078T3 (hu) |
| ES (1) | ES2141089T3 (hu) |
| FI (1) | FI113786B (hu) |
| GR (1) | GR3032804T3 (hu) |
| HK (1) | HK1014732A1 (hu) |
| HU (1) | HU218416B (hu) |
| IE (2) | IE20000918A1 (hu) |
| NO (1) | NO311366B1 (hu) |
| NZ (1) | NZ237532A (hu) |
| PL (3) | PL168235B1 (hu) |
| PT (1) | PT97103B (hu) |
| SK (1) | SK282873B6 (hu) |
| WO (1) | WO1991014775A1 (hu) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IE20000918A1 (en) * | 1990-03-22 | 2001-05-30 | Sloan Kettering Inst Cancer | GP75 As a Tumor Vaccine for Melanoma |
| US7041801B1 (en) * | 1995-06-07 | 2006-05-09 | Vanderbilt University | Antibodies binding to polypeptides encoded by developmentally-regulated endothelial cell locus-1 |
| US7015312B1 (en) | 1996-02-09 | 2006-03-21 | The United States Of America As Represented By The Department Of Health And Human Services | Antibodies to the protein product encoded by ORF3 of the TRP-1 gene and compositions and kits thereof |
| US7001600B1 (en) | 1996-02-09 | 2006-02-21 | The United States Of America As Represented By The Secretary Of Health And Human Services | Identification of TRP-2 as a human tumor antigen recognized by cytotoxic T lymphocytes |
| US6083703A (en) * | 1996-02-09 | 2000-07-04 | The United States Of America As Represented By The Department Of Health And Human Services | Identification of TRP-2 as a human tumor antigen recognized by cytotoxic T lymphocytes |
| US5840839A (en) * | 1996-02-09 | 1998-11-24 | The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services | Alternative open reading frame DNA of a normal gene and a novel human cancer antigen encoded therein |
| AU2001241533A1 (en) * | 2000-02-15 | 2001-08-27 | The Regents Of The University Of California | A universal vaccine and method for treating cancer employing telomerase reverse transcriptase |
| US6613534B2 (en) | 2001-03-20 | 2003-09-02 | Wake Forest University Health Sciences | MAP-2 as a determinant of metastatic potential |
| US20030113919A1 (en) * | 2001-08-17 | 2003-06-19 | Aventis Pasteur, Ltd. | Immunogenic targets for melanoma |
| US20030157720A1 (en) * | 2002-02-06 | 2003-08-21 | Expression Technologies Inc. | Protein standard for estimating size and mass |
| JP5213075B2 (ja) | 2007-06-15 | 2013-06-19 | ジェネラックス・コーポレイション | 腫瘍の画像化および／または処置のための微生物 |
| US7951370B2 (en) | 2008-03-12 | 2011-05-31 | Imclone Llc | Anti-TYRP1 antibodies |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2504010B1 (fr) * | 1981-04-15 | 1985-10-25 | Sanofi Sa | Medicaments anticancereux contenant la chaine a de la ricine associee a un anticorps antimelanome et procede pour leur preparation |
| US4808704A (en) * | 1981-09-30 | 1989-02-28 | Sloan-Kettering Institute For Cancer Research | Monoclonal antibodies to cell surface antigens of human malignant melanoma |
| US4806628A (en) * | 1982-11-30 | 1989-02-21 | Sloan-Kettering Institute For Cancer Research | Monoclonal antibodies against melanocytes |
| US4591572A (en) * | 1983-04-01 | 1986-05-27 | Sloan-Kettering Institute For Cancer Research | Pigmentation associated, differentiation antigen of human melanoma and autologous antibody |
| USH819H (en) * | 1984-04-30 | 1990-09-04 | The United States Of America As Represented By The Secretary Of Energy | Palladium-109 labeled anti-melanoma monoclonal antibodies |
| US4851510A (en) * | 1984-11-30 | 1989-07-25 | Wadley Technologies, Inc. | Monoclonal antibodies to novel melanoma-associated antigens |
| US4798790A (en) * | 1985-07-18 | 1989-01-17 | Sloan-Kettering Institute | Monoclonal antibody specific for a pigmentation associated antigen |
| US5141742A (en) * | 1986-02-07 | 1992-08-25 | Oncogen | Vaccines against melanoma |
| US5262177A (en) * | 1986-02-07 | 1993-11-16 | Oncogen | Recombinant viruses encoding the human melanoma-associated antigen |
| US5009995A (en) * | 1986-10-27 | 1991-04-23 | Sloan-Kettering Institute For Cancer Research | Monoclonal antibodies to melanoma cells |
| US5059523A (en) * | 1988-05-02 | 1991-10-22 | Sloan-Kettering Institute For Cancer Research | Cell-surface glycoproteins of human sarcomas |
| US5009495A (en) * | 1989-05-26 | 1991-04-23 | Williams Robert D | Hinge for eyeglasses |
| DE69033842T2 (de) | 1989-08-04 | 2002-06-20 | Schering Ag | Äusserliche domäne von c-erbb-2:gp75 |
| IE20000918A1 (en) * | 1990-03-22 | 2001-05-30 | Sloan Kettering Inst Cancer | GP75 As a Tumor Vaccine for Melanoma |
| US5262117A (en) * | 1990-10-12 | 1993-11-16 | Centro Sviluppo Settori Impiego S.R.L. | Process for preparing thermoinsulating and/or structural formed articles and products so obtained |
| US6180604B1 (en) * | 1996-08-21 | 2001-01-30 | Micrologix Biotech Inc. | Compositions and methods for treating infections using analogues of indolicidin |
-
1991
- 1991-03-12 IE IE20000918A patent/IE20000918A1/en not_active IP Right Cessation
- 1991-03-12 IE IE082091A patent/IE910820A1/en not_active IP Right Cessation
- 1991-03-21 CZ CS1991760A patent/CZ290278B6/cs not_active IP Right Cessation
- 1991-03-21 PT PT97103A patent/PT97103B/pt not_active IP Right Cessation
- 1991-03-21 SK SK760-91A patent/SK282873B6/sk unknown
- 1991-03-21 NZ NZ237532A patent/NZ237532A/xx unknown
- 1991-03-22 DK DK91908003T patent/DK0522078T3/da active
- 1991-03-22 EP EP91908003A patent/EP0522078B1/en not_active Revoked
- 1991-03-22 PL PL91289550A patent/PL168235B1/pl not_active IP Right Cessation
- 1991-03-22 EP EP99109256A patent/EP0965640A1/en not_active Withdrawn
- 1991-03-22 PL PL91307929A patent/PL169105B1/pl not_active IP Right Cessation
- 1991-03-22 DE DE69131829T patent/DE69131829T2/de not_active Revoked
- 1991-03-22 WO PCT/US1991/001942 patent/WO1991014775A1/en not_active Application Discontinuation
- 1991-03-22 HU HU9203009A patent/HU218416B/hu unknown
- 1991-03-22 AU AU76906/91A patent/AU660412B2/en not_active Ceased
- 1991-03-22 JP JP50783191A patent/JP3336006B2/ja not_active Expired - Fee Related
- 1991-03-22 ES ES91908003T patent/ES2141089T3/es not_active Expired - Lifetime
- 1991-03-22 CA CA002078773A patent/CA2078773C/en not_active Expired - Fee Related
- 1991-03-22 PL PL91307930A patent/PL169168B1/pl not_active IP Right Cessation
- 1991-03-22 AT AT91908003T patent/ATE187493T1/de not_active IP Right Cessation
-
1992
- 1992-09-21 NO NO19923659A patent/NO311366B1/no unknown
- 1992-09-21 FI FI924222A patent/FI113786B/fi active
-
1995
- 1995-03-24 US US08/409,794 patent/US6168946B1/en not_active Expired - Lifetime
-
1998
- 1998-12-28 HK HK98116009A patent/HK1014732A1/xx not_active IP Right Cessation
-
2000
- 2000-02-29 GR GR20000400507T patent/GR3032804T3/el not_active IP Right Cessation
-
2001
- 2001-12-25 JP JP2001391870A patent/JP2002241314A/ja active Pending
-
2004
- 2004-06-25 US US10/877,489 patent/US20050037462A1/en not_active Abandoned
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Jimenez et al. | Specific identification of an authentic clone for mammalian tyrosinase | |
| US5141742A (en) | Vaccines against melanoma | |
| AU775162B2 (en) | Tumor associated antigen peptides and use of same as anti-tumor vaccines | |
| EP0522078B1 (en) | Gp75 as a tumor vaccine for melanoma | |
| WO2003008537A2 (en) | Epitope sequences | |
| Vijayasaradhi et al. | Purification of an autoantigenic 75‐kDa human melanosomal glycoprotein | |
| JP4019040B2 (ja) | 抗原提示の調節 | |
| CA2182889C (en) | Peptides recognized by melanoma-specific cytotoxic lymphocytes, and uses therefor | |
| JP4315257B2 (ja) | 新規コンドロイチン硫酸プロテオグリカン、そのコア蛋白質、それをコードするｄｎａおよびそれに対する抗体 | |
| Nussbaum et al. | Site-specific antibodies to rat myelin proteolipids directed against the C-terminal hexapeptide | |
| Surman et al. | Generation of polyclonal rabbit antisera to mouse melanoma associated antigens using gene gun immunization | |
| JPH09194502A (ja) | 新規コンドロイチン硫酸プロテオグリカン、そのコア蛋白質、それをコードするｄｎａおよびそれに対する抗体 | |
| JPH0751065A (ja) | 糖タンパク質３９遺伝子 | |
| Nagatsu et al. | Antibodies raised against different oligopeptide segments of human dopamine-β-hydroxylase | |
| Amar-Costesec et al. | Identification and characterization of the tumor-specific P1A gene product | |
| EP1369478A1 (en) | Novel scavenger receptor class a protein | |
| Kahn-Perles et al. | Cytotoxic T lymphocyte recognition of secreted HLA class I molecules. | |
| Shiraga et al. | Purification and Characterization of Two AmineN-Sulfotransferases, AST-RB1 (ST3A1) and AST-RB2 (ST2A8), from Liver Cytosols of Male Rabbits | |
| Verdier et al. | Identification of a new, testis-specific sperm antigen localized on the principal piece of the spermatozoa tail in the fox (Vulpes vulpes) | |
| KR20060114326A (ko) | 티로시나아제 돌연변이 및 이의 사용 방법 | |
| WO1991014698A1 (en) | Marine tyrosinase gene | |
| Walker | Characterization of adenylate cyclase toxin plus macrophage and thymic peptides by mass spectrometry | |
| JPH11222499A (ja) | プロテアソーム抑制蛋白質およびそれをコードするポリヌクレオチド |