JPH06506479A - 合成ｈｔｌｖ−２ペプチドを用いるイムノアッセイ - Google Patents

合成ｈｔｌｖ−２ペプチドを用いるイムノアッセイ

Info

Publication number: JPH06506479A
Authority: JP; Japan
Prior art keywords: htlv; sequence identification; solid phase; peptide; amino acid
Prior art date: 1991-11-25
Legal status (The legal status 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 status listed.): Pending

Application number

JP5510159A

Other languages

English (en)

Japanese (ja)

Inventor

シャー，ディニッシュ　オー

ナス，ヌラペンドラ

Original Assignee

デイド、インターナショナル、インコーポレイテッド

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.)

1991-11-25

Filing date

1992-11-20

Publication date

1994-07-21

1992-11-20 Application filed by デイド、インターナショナル、インコーポレイテッド filed Critical デイド、インターナショナル、インコーポレイテッド

1994-07-21 Publication of JPH06506479A publication Critical patent/JPH06506479A/ja

Status Pending legal-status Critical Current

Links

108090000765 processed proteins & peptides Proteins 0.000 title claims description 63
241000714259 Human T-lymphotropic virus 2 Species 0.000 title claims description 15
238000003018 immunoassay Methods 0.000 title description 4
239000007790 solid phase Substances 0.000 claims description 16
102000004196 processed proteins & peptides Human genes 0.000 claims description 11
239000011859 microparticle Substances 0.000 claims description 9
238000000034 method Methods 0.000 claims description 8
210000004369 blood Anatomy 0.000 claims description 5
239000008280 blood Substances 0.000 claims description 5
239000003153 chemical reaction reagent Substances 0.000 claims description 5
230000000405 serological effect Effects 0.000 claims description 5
238000001514 detection method Methods 0.000 claims description 4
239000013642 negative control Substances 0.000 claims description 3
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 claims description 2
125000003275 alpha amino acid group Chemical group 0.000 claims 4
230000001900 immune effect Effects 0.000 claims 3
125000001433 C-terminal amino-acid group Chemical group 0.000 claims 1
150000001875 compounds Chemical class 0.000 claims 1
238000002405 diagnostic procedure Methods 0.000 claims 1
239000002245 particle Substances 0.000 description 39
150000001413 amino acids Chemical class 0.000 description 30
235000001014 amino acid Nutrition 0.000 description 27
241000714260 Human T-lymphotropic virus 1 Species 0.000 description 14
239000002253 acid Substances 0.000 description 13
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 12
238000003556 assay Methods 0.000 description 12
239000000872 buffer Substances 0.000 description 11
150000007513 acids Chemical class 0.000 description 10
239000006228 supernatant Substances 0.000 description 10
BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 8
ZYGHJZDHTFUPRJ-UHFFFAOYSA-N coumarin Chemical compound C1=CC=C2OC(=O)C=CC2=C1 ZYGHJZDHTFUPRJ-UHFFFAOYSA-N 0.000 description 8
206010020460 Human T-cell lymphotropic virus type I infection Diseases 0.000 description 7
230000005298 paramagnetic effect Effects 0.000 description 7
229920001213 Polysorbate 20 Polymers 0.000 description 6
PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 6
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 6
239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 6
235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 6
210000002966 serum Anatomy 0.000 description 6
239000000243 solution Substances 0.000 description 6
RWCOTTLHDJWHRS-YUMQZZPRSA-N Pro-Pro Chemical compound OC(=O)[C@@H]1CCCN1C(=O)[C@H]1NCCC1 RWCOTTLHDJWHRS-YUMQZZPRSA-N 0.000 description 5
UPUNWAXSLPBMRK-XTWBLICNSA-N Trp-Thr-Thr Chemical compound [H]N[C@@H](CC1=CNC2=C1C=CC=C2)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O UPUNWAXSLPBMRK-XTWBLICNSA-N 0.000 description 5
108010077112 prolyl-proline Proteins 0.000 description 5
239000000523 sample Substances 0.000 description 5
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
QOLYAJSZHIJCTO-VQVTYTSYSA-N Thr-Pro Chemical compound C[C@@H](O)[C@H](N)C(=O)N1CCC[C@H]1C(O)=O QOLYAJSZHIJCTO-VQVTYTSYSA-N 0.000 description 4
239000007975 buffered saline Substances 0.000 description 4
229960000956 coumarin Drugs 0.000 description 4
235000001671 coumarin Nutrition 0.000 description 4
239000006148 magnetic separator Substances 0.000 description 4
108090000623 proteins and genes Proteins 0.000 description 4
239000011780 sodium chloride Substances 0.000 description 4
HKTRDWYCAUTRRL-YUMQZZPRSA-N Glu-His Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CN=CN1 HKTRDWYCAUTRRL-YUMQZZPRSA-N 0.000 description 3
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
241000700605 Viruses Species 0.000 description 3
102000005936 beta-Galactosidase Human genes 0.000 description 3
108010005774 beta-Galactosidase Proteins 0.000 description 3
230000008878 coupling Effects 0.000 description 3
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239000001488 sodium phosphate Substances 0.000 description 3
229910000162 sodium phosphate Inorganic materials 0.000 description 3
239000000758 substrate Substances 0.000 description 3
238000012360 testing method Methods 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
HSPSXROIMXIJQW-BQBZGAKWSA-N Asp-His Chemical compound OC(=O)C[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CNC=N1 HSPSXROIMXIJQW-BQBZGAKWSA-N 0.000 description 2
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PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
239000004472 Lysine Substances 0.000 description 2
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
SEQKRHFRPICQDD-UHFFFAOYSA-N N-tris(hydroxymethyl)methylglycine Chemical compound OCC(CO)(CO)[NH2+]CC([O-])=O SEQKRHFRPICQDD-UHFFFAOYSA-N 0.000 description 2
FYXCBXDAMPEHIQ-FHWLQOOXSA-N Pro-Trp-Lys Chemical compound C1C[C@H](NC1)C(=O)N[C@@H](CC2=CNC3=CC=CC=C32)C(=O)N[C@@H](CCCCN)C(=O)O FYXCBXDAMPEHIQ-FHWLQOOXSA-N 0.000 description 2
BNQVUHQWZGTIBX-IUCAKERBSA-N Val-His Chemical compound CC(C)[C@H]([NH3+])C(=O)N[C@H](C([O-])=O)CC1=CN=CN1 BNQVUHQWZGTIBX-IUCAKERBSA-N 0.000 description 2
125000000539 amino acid group Chemical group 0.000 description 2
RDOXTESZEPMUJZ-UHFFFAOYSA-N anisole Chemical compound COC1=CC=CC=C1 RDOXTESZEPMUJZ-UHFFFAOYSA-N 0.000 description 2
230000015572 biosynthetic process Effects 0.000 description 2
210000004027 cell Anatomy 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
235000018417 cysteine Nutrition 0.000 description 2
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
QEWYKACRFQMRMB-UHFFFAOYSA-N fluoroacetic acid Chemical compound OC(=O)CF QEWYKACRFQMRMB-UHFFFAOYSA-N 0.000 description 2
238000004128 high performance liquid chromatography Methods 0.000 description 2
JXDYKVIHCLTXOP-UHFFFAOYSA-N isatin Chemical compound C1=CC=C2C(=O)C(=O)NC2=C1 JXDYKVIHCLTXOP-UHFFFAOYSA-N 0.000 description 2
238000005259 measurement Methods 0.000 description 2
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
239000000047 product Substances 0.000 description 2
235000018102 proteins Nutrition 0.000 description 2
102000004169 proteins and genes Human genes 0.000 description 2
239000002002 slurry Substances 0.000 description 2
KZNICNPSHKQLFF-UHFFFAOYSA-N succinimide Chemical compound O=C1CCC(=O)N1 KZNICNPSHKQLFF-UHFFFAOYSA-N 0.000 description 2
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
238000005406 washing Methods 0.000 description 2
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
BDNKZNFMNDZQMI-UHFFFAOYSA-N 1,3-diisopropylcarbodiimide Chemical compound CC(C)N=C=NC(C)C BDNKZNFMNDZQMI-UHFFFAOYSA-N 0.000 description 1
SPBDXSGPUHCETR-JFUDTMANSA-N 8883yp2r6d Chemical compound O1[C@@H](C)[C@H](O)[C@@H](OC)C[C@@H]1O[C@@H]1[C@@H](OC)C[C@H](O[C@@H]2C(=C/C[C@@H]3C[C@@H](C[C@@]4(O[C@@H]([C@@H](C)CC4)C(C)C)O3)OC(=O)[C@@H]3C=C(C)[C@@H](O)[C@H]4OC\C([C@@]34O)=C/C=C/[C@@H]2C)/C)O[C@H]1C.C1C[C@H](C)[C@@H]([C@@H](C)CC)O[C@@]21O[C@H](C\C=C(C)\[C@@H](O[C@@H]1O[C@@H](C)[C@H](O[C@@H]3O[C@@H](C)[C@H](O)[C@@H](OC)C3)[C@@H](OC)C1)[C@@H](C)\C=C\C=C/1[C@]3([C@H](C(=O)O4)C=C(C)[C@@H](O)[C@H]3OC\1)O)C[C@H]4C2 SPBDXSGPUHCETR-JFUDTMANSA-N 0.000 description 1
208000009746 Adult T-Cell Leukemia-Lymphoma Diseases 0.000 description 1
208000016683 Adult T-cell leukemia/lymphoma Diseases 0.000 description 1
OLVCTPPSXNRGKV-GUBZILKMSA-N Ala-Pro-Pro Chemical compound C[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(O)=O)CCC1 OLVCTPPSXNRGKV-GUBZILKMSA-N 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
101100129088 Caenorhabditis elegans lys-2 gene Proteins 0.000 description 1
VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
JHQHHFDFGWOFNR-UHFFFAOYSA-N Cl.[N-]=[N+]=[N-].[Na+] Chemical compound Cl.[N-]=[N+]=[N-].[Na+] JHQHHFDFGWOFNR-UHFFFAOYSA-N 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
102000003886 Glycoproteins Human genes 0.000 description 1
108090000288 Glycoproteins Proteins 0.000 description 1
MDCTVRUPVLZSPG-BQBZGAKWSA-N His-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CNC=N1 MDCTVRUPVLZSPG-BQBZGAKWSA-N 0.000 description 1
ZZLWLWSUIBSMNP-CIUDSAMLSA-N His-Asp-Ser Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(O)=O ZZLWLWSUIBSMNP-CIUDSAMLSA-N 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
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
OTXBNHIUIHNGAO-UWVGGRQHSA-N Leu-Lys Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(O)=O)CCCCN OTXBNHIUIHNGAO-UWVGGRQHSA-N 0.000 description 1
MUCIDQMDOYQYBR-IHRRRGAJSA-N Leu-Pro-His Chemical compound CC(C)C[C@@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC2=CN=CN2)C(=O)O)N MUCIDQMDOYQYBR-IHRRRGAJSA-N 0.000 description 1
LRKCBIUDWAXNEG-CSMHCCOUSA-N Leu-Thr Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(O)=O LRKCBIUDWAXNEG-CSMHCCOUSA-N 0.000 description 1
241000287462 Phalacrocorax carbo Species 0.000 description 1
239000004793 Polystyrene Substances 0.000 description 1
BEPSGCXDIVACBU-IUCAKERBSA-N Pro-His Chemical compound C([C@@H](C(=O)O)NC(=O)[C@H]1NCCC1)C1=CN=CN1 BEPSGCXDIVACBU-IUCAKERBSA-N 0.000 description 1
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
108091006503 SLC26A1 Proteins 0.000 description 1
101800001271 Surface protein Proteins 0.000 description 1
108010008038 Synthetic Vaccines Proteins 0.000 description 1
UZMAPBJVXOGOFT-UHFFFAOYSA-N Syringetin Natural products COC1=C(O)C(OC)=CC(C2=C(C(=O)C3=C(O)C=C(O)C=C3O2)O)=C1 UZMAPBJVXOGOFT-UHFFFAOYSA-N 0.000 description 1
210000001744 T-lymphocyte Anatomy 0.000 description 1
KERCOYANYUPLHJ-XGEHTFHBSA-N Thr-Pro-Ser Chemical compound C[C@@H](O)[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(O)=O KERCOYANYUPLHJ-XGEHTFHBSA-N 0.000 description 1
101800000385 Transmembrane protein Proteins 0.000 description 1
239000007997 Tricine buffer Substances 0.000 description 1
SYFHQHYTNCQCCN-MELADBBJSA-N Tyr-Ser-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CO)NC(=O)[C@H](CC2=CC=C(C=C2)O)N)C(=O)O SYFHQHYTNCQCCN-MELADBBJSA-N 0.000 description 1
WJVLTYSHNXRCLT-NHCYSSNCSA-N Val-His-Asp Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CC(=O)O)C(=O)O)N WJVLTYSHNXRCLT-NHCYSSNCSA-N 0.000 description 1
230000006978 adaptation Effects 0.000 description 1
201000006966 adult T-cell leukemia Diseases 0.000 description 1
150000001336 alkenes Chemical class 0.000 description 1
150000001408 amides Chemical group 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
239000000427 antigen Substances 0.000 description 1
230000000890 antigenic effect Effects 0.000 description 1
102000036639 antigens Human genes 0.000 description 1
108091007433 antigens Proteins 0.000 description 1
238000003491 array Methods 0.000 description 1
239000012888 bovine serum Substances 0.000 description 1
239000007853 buffer solution Substances 0.000 description 1
238000006243 chemical reaction Methods 0.000 description 1
238000004140 cleaning Methods 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
239000003599 detergent Substances 0.000 description 1
238000011161 development Methods 0.000 description 1
229940061607 dibasic sodium phosphate Drugs 0.000 description 1
KCFYHBSOLOXZIF-UHFFFAOYSA-N dihydrochrysin Natural products COC1=C(O)C(OC)=CC(C2OC3=CC(O)=CC(O)=C3C(=O)C2)=C1 KCFYHBSOLOXZIF-UHFFFAOYSA-N 0.000 description 1
239000012470 diluted sample Substances 0.000 description 1
239000003085 diluting agent Substances 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
201000010099 disease Diseases 0.000 description 1
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
229940079593 drug Drugs 0.000 description 1
239000003814 drug Substances 0.000 description 1
238000011156 evaluation Methods 0.000 description 1
230000005284 excitation Effects 0.000 description 1
230000001815 facial effect Effects 0.000 description 1
235000011187 glycerol Nutrition 0.000 description 1
230000028993 immune response Effects 0.000 description 1
230000006872 improvement Effects 0.000 description 1
238000011534 incubation Methods 0.000 description 1
239000003112 inhibitor Substances 0.000 description 1
238000001990 intravenous administration Methods 0.000 description 1
210000003127 knee Anatomy 0.000 description 1
238000002372 labelling Methods 0.000 description 1
108010034529 leucyl-lysine Proteins 0.000 description 1
229910001629 magnesium chloride Inorganic materials 0.000 description 1
230000005291 magnetic effect Effects 0.000 description 1
UZKWTJUDCOPSNM-UHFFFAOYSA-N methoxybenzene Substances CCCCOC=C UZKWTJUDCOPSNM-UHFFFAOYSA-N 0.000 description 1
238000012986 modification Methods 0.000 description 1
230000004048 modification Effects 0.000 description 1
108091005601 modified peptides Proteins 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
JRZJOMJEPLMPRA-UHFFFAOYSA-N olefin Natural products CCCCCCCC=C JRZJOMJEPLMPRA-UHFFFAOYSA-N 0.000 description 1
230000001717 pathogenic effect Effects 0.000 description 1
238000010647 peptide synthesis reaction Methods 0.000 description 1
239000012071 phase Substances 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
229920000136 polysorbate Polymers 0.000 description 1
229920002223 polystyrene Polymers 0.000 description 1
230000007017 scission Effects 0.000 description 1
238000011896 sensitive detection Methods 0.000 description 1
238000009589 serological test Methods 0.000 description 1
230000001568 sexual effect Effects 0.000 description 1
239000011734 sodium Substances 0.000 description 1
229910052708 sodium Inorganic materials 0.000 description 1
SRWFBFUYENBCGF-UHFFFAOYSA-M sodium;chloride;hydrochloride Chemical compound [Na+].Cl.[Cl-] SRWFBFUYENBCGF-UHFFFAOYSA-M 0.000 description 1
238000002764 solid phase assay Methods 0.000 description 1
238000001179 sorption measurement Methods 0.000 description 1
238000001228 spectrum Methods 0.000 description 1
229960002317 succinimide Drugs 0.000 description 1
239000000725 suspension Substances 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
HNKJADCVZUBCPG-UHFFFAOYSA-N thioanisole Chemical compound CSC1=CC=CC=C1 HNKJADCVZUBCPG-UHFFFAOYSA-N 0.000 description 1
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229920002554 vinyl polymer Polymers 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/569—Immunoassay; Biospecific binding assay; Materials therefor for microorganisms, e.g. protozoa, bacteria, viruses
- G01N33/56983—Viruses
- G01N33/56988—HIV or HTLV
- 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
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/14011—Deltaretrovirus, e.g. bovine leukeamia virus
- C12N2740/14022—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Virology (AREA)
Molecular Biology (AREA)
Immunology (AREA)
Engineering & Computer Science (AREA)
Biomedical Technology (AREA)
Medicinal Chemistry (AREA)
Organic Chemistry (AREA)
Hematology (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
Urology & Nephrology (AREA)
Analytical Chemistry (AREA)
General Physics & Mathematics (AREA)
AIDS & HIV (AREA)
Physics & Mathematics (AREA)
Biotechnology (AREA)
Tropical Medicine & Parasitology (AREA)
Microbiology (AREA)
Food Science & Technology (AREA)
Pathology (AREA)
Gastroenterology & Hepatology (AREA)
Biophysics (AREA)
Genetics & Genomics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Cell Biology (AREA)
Peptides Or Proteins (AREA)

JP5510159A 1991-11-25 1992-11-20 合成ｈｔｌｖ−２ペプチドを用いるイムノアッセイ Pending JPH06506479A (ja)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
US79755791A	1991-11-25	1991-11-25
US797,557		1991-11-25
PCT/US1992/009973 WO1993011431A1 (en)	1991-11-25	1992-11-20	Immunoassay using synthetic htlv-ii peptides

Publications (1)

Publication Number	Publication Date
JPH06506479A true JPH06506479A (ja)	1994-07-21

Family

ID=25171175

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP5510159A Pending JPH06506479A (ja)	1991-11-25	1992-11-20	合成ｈｔｌｖ−２ペプチドを用いるイムノアッセイ

Country Status (5)

Country	Link
EP (1)	EP0573630A4 (de)
JP (1)	JPH06506479A (de)
AU (1)	AU660752B2 (de)
CA (1)	CA2100883A1 (de)
WO (1)	WO1993011431A1 (de)

Families Citing this family (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA2117378C (en) *	1992-02-24	2003-04-15	Steven K. H. Foung	Htlv-i/htlv-ii assay and method
US7166439B2 (en) *	2002-03-01	2007-01-23	Gmp Endotherapeutics, Inc.	Assay for anti-INGAP antibodies

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* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4070246A (en) *	1976-04-09	1978-01-24	Abbott Laboratories	Reactive matrices
US4070247A (en) *	1977-03-30	1978-01-24	Indiana University Foundation	Diagnostic media
US5039604A (en) *	1987-08-21	1991-08-13	Cellular Products, Inc.	Test device and method of preparing same, assay kit and method for the simultaneous detection of two HTLV or HIV antibodies
US4847325A (en) *	1988-01-20	1989-07-11	Cetus Corporation	Conjugation of polymer to colony stimulating factor-1
SE8900721D0 (sv) *	1989-03-02	1989-03-02	Blomberg Jonas	Methods for detection of antibodies to
FI910245L (fi) *	1990-01-24	1991-07-25	United Biomedical Inc	Syntetiska peptidkompositioner med immunoreaktivitet mot htlv-antikroppar.
NZ238855A (en) *	1990-07-18	1994-03-25	Iaf Biochem Int	Peptides, mixtures thereof and compositions useful for detecting htlv-i and htlv-ii infections

1992
- 1992-11-20 CA CA 2100883 patent/CA2100883A1/en not_active Abandoned
- 1992-11-20 JP JP5510159A patent/JPH06506479A/ja active Pending
- 1992-11-20 WO PCT/US1992/009973 patent/WO1993011431A1/en not_active Ceased
- 1992-11-20 AU AU31425/93A patent/AU660752B2/en not_active Ceased
- 1992-11-20 EP EP92925329A patent/EP0573630A4/de not_active Withdrawn

Also Published As

Publication number	Publication date
AU660752B2 (en)	1995-07-06
EP0573630A4 (de)	1995-07-12
EP0573630A1 (de)	1993-12-15
AU3142593A (en)	1993-06-28
CA2100883A1 (en)	1993-05-26
WO1993011431A1 (en)	1993-06-10

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EP0891982B1 (de)	2007-06-13	HIV-Peptide
CA2005955C (en)	2000-10-24	Synthetic hiv-like peptides, their compositions and uses
JPH05503722A (ja)	1993-06-17	Ｃ型肝炎ウイルスに対する抗体を検出するための合成抗原
EP0284587A2 (de)	1988-09-28	Synthetische Peptid-Antigene für den Nachweis von HIV-1-Infektionen
JPH0751598B2 (ja)	1995-06-05	Ｈｔｌｖ‐１感染検出用合成ペプチド抗原
EP0267802A2 (de)	1988-05-18	Synthetisches Antigen zum Nachweis von mit AIDS in Zusammenhang stehenden Krankheiten
JP3020289B2 (ja)	2000-03-15	Ｈｉｖウイルス類のエンベロープ糖タンパク質由来のペプチド、これらのウイルスによって起こる感染の検出とエイズ症に対する予防接種へのこれらペプチドの用途
US5260189A (en)	1993-11-09	Synthetic HIV-like peptides their compositions and uses
EP0247557B1 (de)	1994-04-20	HTLV-III(LAV)Decke-Peptide
US6649735B1 (en)	2003-11-18	Process for the determination of peptides corresponding to immunologically important epitopes and their use in a process for determination of antibodies or biotinylated peptides corresponding to immunologically important epitopes, a process for preparing them and compositions containing them
EP0710294A1 (de)	1996-05-08	Lineare und verzweigte peptide für die diagnose und bestimmung von non-a, non-b hepatitis
JPH06506479A (ja)	1994-07-21	合成ｈｔｌｖ−２ペプチドを用いるイムノアッセイ
AU657590B2 (en)	1995-03-16	Synthetic peptides corresponding to portions of HIV-2 virus and methods of using in an improved assay
JPH08320324A (ja)	1996-12-03	口蹄疫診断用ペプチドおよび当該ペプチドを含有する口蹄疫診断用抗原
AU640569B2 (en)	1993-08-26	Assay for non-a non-b hepatitis
JPH02111791A (ja)	1990-04-24	Ｈｉｖ抗体と免疫化学的に反応する合成ポリペプチド
US20030108974A1 (en)	2003-06-12	Method for serological typing using type-specific antigens
JPH02209891A (ja)	1990-08-21	新規ペプチド
JPH02218693A (ja)	1990-08-31	新規ペプチド
JPH11508036A (ja)	1999-07-13	抗−ｈｉｖ−１または抗−ｈｉｖ−２抗体を検出するための改良されたハプテン−ペプチド結合物
DE DK et al.	0	HCV MOSAIK ANTIGEN ZUSAMMENSETZUNG COMPOSITION D’ANTIGENE MOSAIQUE DU VIRUS DE L’HEPATITE C (VHC)