TW581812B - Assay for the diagnosis of schizophrenia based on a new peptide - Google Patents
Assay for the diagnosis of schizophrenia based on a new peptide Download PDFInfo
- Publication number
- TW581812B TW581812B TW088105128A TW88105128A TW581812B TW 581812 B TW581812 B TW 581812B TW 088105128 A TW088105128 A TW 088105128A TW 88105128 A TW88105128 A TW 88105128A TW 581812 B TW581812 B TW 581812B
- Authority
- TW
- Taiwan
- Prior art keywords
- sequence
- peptide
- patent application
- identification number
- sequence identification
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 120
- 201000000980 schizophrenia Diseases 0.000 title claims abstract description 40
- 238000003745 diagnosis Methods 0.000 title abstract description 3
- 238000003556 assay Methods 0.000 title 1
- 150000001413 amino acids Chemical class 0.000 claims abstract description 48
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 32
- 230000000698 schizophrenic effect Effects 0.000 claims abstract description 23
- 210000001124 body fluid Anatomy 0.000 claims abstract description 11
- 239000010839 body fluid Substances 0.000 claims abstract description 11
- 230000002209 hydrophobic effect Effects 0.000 claims abstract description 5
- 230000027455 binding Effects 0.000 claims description 44
- 239000012634 fragment Substances 0.000 claims description 18
- MUSGYEMSJUFFHT-UWABRSFTSA-N 2-[(4R,7S,10S,13S,19S,22S,25S,28S,31S,34R)-34-[[(2S,3S)-2-[[(2R)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-4-[[(2S,3S)-1-amino-3-methyl-1-oxopentan-2-yl]-methylcarbamoyl]-25-(3-amino-3-oxopropyl)-7-(3-carbamimidamidopropyl)-10-(1H-imidazol-5-ylmethyl)-19-(1H-indol-3-ylmethyl)-13,17-dimethyl-28-[(1-methylindol-3-yl)methyl]-6,9,12,15,18,21,24,27,30,33-decaoxo-31-propan-2-yl-1,2-dithia-5,8,11,14,17,20,23,26,29,32-decazacyclopentatriacont-22-yl]acetic acid Chemical compound CC[C@H](C)[C@H](NC(=O)[C@H](N)Cc1ccc(O)cc1)C(=O)N[C@H]1CSSC[C@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](Cc2cnc[nH]2)NC(=O)[C@H](C)NC(=O)CN(C)C(=O)[C@H](Cc2c[nH]c3ccccc23)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc2cn(C)c3ccccc23)NC(=O)[C@@H](NC1=O)C(C)C)C(=O)N(C)[C@@H]([C@@H](C)CC)C(N)=O MUSGYEMSJUFFHT-UWABRSFTSA-N 0.000 claims description 7
- 108060003951 Immunoglobulin Proteins 0.000 claims description 3
- 239000003153 chemical reaction reagent Substances 0.000 claims description 3
- 102000018358 immunoglobulin Human genes 0.000 claims description 3
- 239000013589 supplement Substances 0.000 claims 1
- 230000000890 antigenic effect Effects 0.000 abstract description 2
- 235000001014 amino acid Nutrition 0.000 description 41
- 235000018102 proteins Nutrition 0.000 description 21
- 102000004169 proteins and genes Human genes 0.000 description 21
- 108090000623 proteins and genes Proteins 0.000 description 21
- 238000011049 filling Methods 0.000 description 18
- 238000000034 method Methods 0.000 description 15
- 230000000692 anti-sense effect Effects 0.000 description 14
- JHNOXVASMSXSNB-WEDXCCLWSA-N Lys-Thr-Gly Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(O)=O JHNOXVASMSXSNB-WEDXCCLWSA-N 0.000 description 13
- AEFJNECXZCODJM-UWVGGRQHSA-N Val-Val-Gly Chemical compound CC(C)[C@H]([NH3+])C(=O)N[C@@H](C(C)C)C(=O)NCC([O-])=O AEFJNECXZCODJM-UWVGGRQHSA-N 0.000 description 12
- 108010050848 glycylleucine Proteins 0.000 description 12
- 210000002381 plasma Anatomy 0.000 description 11
- FOEHRHOBWFQSNW-KATARQTJSA-N Leu-Cys-Thr Chemical compound C[C@H]([C@@H](C(=O)O)NC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)N)O FOEHRHOBWFQSNW-KATARQTJSA-N 0.000 description 10
- 230000002079 cooperative effect Effects 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 102000012288 Phosphopyruvate Hydratase Human genes 0.000 description 9
- 108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 9
- 102000004190 Enzymes Human genes 0.000 description 8
- 108090000790 Enzymes Proteins 0.000 description 8
- VPZXBVLAVMBEQI-UHFFFAOYSA-N glycyl-DL-alpha-alanine Natural products OC(=O)C(C)NC(=O)CN VPZXBVLAVMBEQI-UHFFFAOYSA-N 0.000 description 8
- 108010061238 threonyl-glycine Proteins 0.000 description 8
- 210000004369 blood Anatomy 0.000 description 7
- 239000008280 blood Substances 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- DYJJJCHDHLEFDW-FXQIFTODSA-N Ala-Pro-Cys Chemical compound C[C@@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CS)C(=O)O)N DYJJJCHDHLEFDW-FXQIFTODSA-N 0.000 description 6
- AIZVVCMAFRREQS-GUBZILKMSA-N Pro-Cys-Arg Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O AIZVVCMAFRREQS-GUBZILKMSA-N 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- 239000000427 antigen Substances 0.000 description 6
- 102000036639 antigens Human genes 0.000 description 6
- 108091007433 antigens Proteins 0.000 description 6
- 229940127236 atypical antipsychotics Drugs 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 5
- 239000003146 anticoagulant agent Substances 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- ZIWWTZWAKYBUOB-CIUDSAMLSA-N Ala-Asp-Leu Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O ZIWWTZWAKYBUOB-CIUDSAMLSA-N 0.000 description 4
- ALNKNYKSZPSLBD-ZDLURKLDSA-N Cys-Thr-Gly Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(O)=O ALNKNYKSZPSLBD-ZDLURKLDSA-N 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- KZNQNBZMBZJQJO-UHFFFAOYSA-N N-glycyl-L-proline Natural products NCC(=O)N1CCCC1C(O)=O KZNQNBZMBZJQJO-UHFFFAOYSA-N 0.000 description 4
- ALJGSKMBIUEJOB-FXQIFTODSA-N Pro-Ala-Cys Chemical compound C[C@@H](C(=O)N[C@@H](CS)C(=O)O)NC(=O)[C@@H]1CCCN1 ALJGSKMBIUEJOB-FXQIFTODSA-N 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 239000000539 dimer Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 239000013642 negative control Substances 0.000 description 4
- 210000004623 platelet-rich plasma Anatomy 0.000 description 4
- 229920002401 polyacrylamide Polymers 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 3
- 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 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 239000002033 PVDF binder Substances 0.000 description 3
- 229920002125 Sokalan® Polymers 0.000 description 3
- 230000000702 anti-platelet effect Effects 0.000 description 3
- 238000004364 calculation method Methods 0.000 description 3
- 238000004590 computer program Methods 0.000 description 3
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 230000006862 enzymatic digestion Effects 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 238000010998 test method Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical group N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- 101710113670 Anaerobic glycerol-3-phosphate dehydrogenase subunit A Proteins 0.000 description 2
- 101710113668 Anaerobic glycerol-3-phosphate dehydrogenase subunit C Proteins 0.000 description 2
- 101710088194 Dehydrogenase Proteins 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 102000003745 Hepatocyte Growth Factor Human genes 0.000 description 2
- 108090000100 Hepatocyte Growth Factor Proteins 0.000 description 2
- NTYJJOPFIAHURM-UHFFFAOYSA-N Histamine Chemical compound NCCC1=CN=CN1 NTYJJOPFIAHURM-UHFFFAOYSA-N 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 102000011782 Keratins Human genes 0.000 description 2
- 108010076876 Keratins Proteins 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- MIJWOJAXARLEHA-WDSKDSINSA-N Ser-Gly-Glu Chemical compound OC[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CCC(O)=O MIJWOJAXARLEHA-WDSKDSINSA-N 0.000 description 2
- LGNBRHZANHMZHK-NUMRIWBASA-N Thr-Glu-Asp Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CC(=O)O)C(=O)O)N)O LGNBRHZANHMZHK-NUMRIWBASA-N 0.000 description 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- 239000013504 Triton X-100 Substances 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 108010087924 alanylproline Proteins 0.000 description 2
- 229940127219 anticoagulant drug Drugs 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 230000000875 corresponding effect Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 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 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 150000002085 enols Chemical class 0.000 description 2
- 239000000499 gel 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
- 230000005965 immune activity Effects 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 125000002924 primary amino group Chemical class [H]N([H])* 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 238000004007 reversed phase HPLC Methods 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- KPYXMALABCDPGN-HYOZMBHHSA-N (4s)-5-[[(2s)-6-amino-1-[[(2s,3s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2r)-1-[[2-[[2-[[(1s)-3-amino-1-carboxy-3-oxopropyl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]a Chemical compound NC(=O)C[C@@H](C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN)CC1=CC=C(O)C=C1 KPYXMALABCDPGN-HYOZMBHHSA-N 0.000 description 1
- XIYDWQMQCFVXKJ-UHFFFAOYSA-N 4-(chloroamino)phenol Chemical compound OC1=CC=C(NCl)C=C1 XIYDWQMQCFVXKJ-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 208000002109 Argyria Diseases 0.000 description 1
- QNMKWNONJGKJJC-NHCYSSNCSA-N Asp-Leu-Val Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(O)=O QNMKWNONJGKJJC-NHCYSSNCSA-N 0.000 description 1
- 108700016171 Aspartate ammonia-lyases Proteins 0.000 description 1
- 206010050245 Autoimmune thrombocytopenia Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- OBMZMSLWNNWEJA-XNCRXQDQSA-N C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 Chemical compound C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 OBMZMSLWNNWEJA-XNCRXQDQSA-N 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 102000013830 Calcium-Sensing Receptors Human genes 0.000 description 1
- 108010050543 Calcium-Sensing Receptors Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- RGTVXXNMOGHRAY-WDSKDSINSA-N Cys-Arg Chemical compound SC[C@H](N)C(=O)N[C@H](C(O)=O)CCCN=C(N)N RGTVXXNMOGHRAY-WDSKDSINSA-N 0.000 description 1
- MNQZXJOMYWMBOU-VKHMYHEASA-N D-glyceraldehyde Chemical compound OC[C@@H](O)C=O MNQZXJOMYWMBOU-VKHMYHEASA-N 0.000 description 1
- 206010012239 Delusion Diseases 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 206010014557 Emotional poverty Diseases 0.000 description 1
- 208000034826 Genetic Predisposition to Disease Diseases 0.000 description 1
- 206010019070 Hallucination, auditory Diseases 0.000 description 1
- 208000004547 Hallucinations Diseases 0.000 description 1
- AZYBQXPITOLDBL-ISFWSWAHSA-N Heimidine Natural products O(C)c1c(OC)cc2-c3c(O)ccc([C@@H](O)CC(=O)O[C@@H]4C[C@H](N5[C@@H](C4)CCCC5)c2c1)c3 AZYBQXPITOLDBL-ISFWSWAHSA-N 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 241000668842 Lepidosaphes gloverii Species 0.000 description 1
- HRNLUBSXIHFDHP-UHFFFAOYSA-N N-(2-aminophenyl)-4-[[[4-(3-pyridinyl)-2-pyrimidinyl]amino]methyl]benzamide Chemical compound NC1=CC=CC=C1NC(=O)C(C=C1)=CC=C1CNC1=NC=CC(C=2C=NC=CC=2)=N1 HRNLUBSXIHFDHP-UHFFFAOYSA-N 0.000 description 1
- 206010029216 Nervousness Diseases 0.000 description 1
- AZYBQXPITOLDBL-SJQULFJYSA-N O(C)c1c(OC)cc2-c3c(O)ccc([C@H](O)CC(=O)O[C@@H]4C[C@H](N5[C@H](C4)CCCC5)c2c1)c3 Chemical compound O(C)c1c(OC)cc2-c3c(O)ccc([C@H](O)CC(=O)O[C@@H]4C[C@H](N5[C@H](C4)CCCC5)c2c1)c3 AZYBQXPITOLDBL-SJQULFJYSA-N 0.000 description 1
- 101710176384 Peptide 1 Proteins 0.000 description 1
- 206010037180 Psychiatric symptoms Diseases 0.000 description 1
- 208000001431 Psychomotor Agitation Diseases 0.000 description 1
- 208000028017 Psychotic disease Diseases 0.000 description 1
- 206010038743 Restlessness Diseases 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 238000000692 Student's t-test Methods 0.000 description 1
- 208000031981 Thrombocytopenic Idiopathic Purpura Diseases 0.000 description 1
- URIRWLJVWHYLET-ONGXEEELSA-N Val-Gly-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)CNC(=O)[C@@H](N)C(C)C URIRWLJVWHYLET-ONGXEEELSA-N 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003086 colorant Substances 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 238000005094 computer simulation Methods 0.000 description 1
- 125000004122 cyclic group Chemical group 0.000 description 1
- 231100000868 delusion Toxicity 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 229960001340 histamine Drugs 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000001819 mass spectrum Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000003340 mental effect Effects 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 208000022821 personality disease Diseases 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 230000035935 pregnancy Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 208000020016 psychiatric disease Diseases 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 208000022610 schizoaffective disease Diseases 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 208000017520 skin disease Diseases 0.000 description 1
- 229910000033 sodium borohydride Inorganic materials 0.000 description 1
- 239000012279 sodium borohydride Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 229940070710 valerate Drugs 0.000 description 1
- NQPDZGIKBAWPEJ-UHFFFAOYSA-N valeric acid Chemical compound CCCCC(O)=O NQPDZGIKBAWPEJ-UHFFFAOYSA-N 0.000 description 1
- 230000009385 viral infection Effects 0.000 description 1
- 238000003809 water extraction Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/88—Lyases (4.)
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| IL12392598 | 1998-04-02 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| TW581812B true TW581812B (en) | 2004-04-01 |
Family
ID=11071395
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW088105128A TW581812B (en) | 1998-04-02 | 1999-03-31 | Assay for the diagnosis of schizophrenia based on a new peptide |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US7098304B1 (https=) |
| EP (1) | EP1068303B1 (https=) |
| JP (1) | JP4364433B2 (https=) |
| CN (1) | CN1171995C (https=) |
| AR (1) | AR014811A1 (https=) |
| AT (1) | ATE309335T1 (https=) |
| AU (1) | AU3165599A (https=) |
| BR (1) | BR9909308B1 (https=) |
| CA (1) | CA2324380C (https=) |
| DE (1) | DE69928236T2 (https=) |
| IL (1) | IL138746A (https=) |
| TW (1) | TW581812B (https=) |
| WO (1) | WO1999051725A2 (https=) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1331481A4 (en) * | 2000-10-31 | 2005-06-29 | Japan Government | KIT FOR THE DIAGNOSIS OF SCHIZOPHRENIA |
| EP1415162B1 (en) * | 2001-03-21 | 2011-05-11 | Yeda Research And Development Co., Ltd. | Novel peptides for the diagnosis of schizophrenia |
| CN1300588C (zh) * | 2005-02-28 | 2007-02-14 | 上海交通大学 | 用于精神分裂症诊断的血浆特异性蛋白获取方法及应用 |
| WO2007091881A2 (en) * | 2005-04-29 | 2007-08-16 | Leiden University Medical Center | Methods and means for detection of mycobacterium leprae infections |
| ES3038398T3 (en) * | 2015-07-14 | 2025-10-13 | Yeda Res & Dev | Peptide combinations for use in the diagnosis of schizophrenia |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU6913994A (en) | 1993-05-13 | 1994-12-12 | New York University | Psychosis protecting nucleic acid, peptides, compositions and method of use |
| US6008001A (en) * | 1993-11-05 | 1999-12-28 | Yeda Research And Development Co. Ltd. | Diagnosis of the susceptibility of contracting schizophrenia |
| AU695043B2 (en) | 1994-03-01 | 1998-08-06 | Yeda Research And Development Co. Ltd. | Assay for the diagnosis of schizophrenia |
-
1999
- 1999-03-30 EP EP99913557A patent/EP1068303B1/en not_active Expired - Lifetime
- 1999-03-30 AU AU31655/99A patent/AU3165599A/en not_active Abandoned
- 1999-03-30 CA CA002324380A patent/CA2324380C/en not_active Expired - Fee Related
- 1999-03-30 US US09/647,457 patent/US7098304B1/en not_active Expired - Lifetime
- 1999-03-30 WO PCT/IL1999/000190 patent/WO1999051725A2/en not_active Ceased
- 1999-03-30 DE DE69928236T patent/DE69928236T2/de not_active Expired - Lifetime
- 1999-03-30 CN CNB998059951A patent/CN1171995C/zh not_active Expired - Fee Related
- 1999-03-30 BR BRPI9909308-1A patent/BR9909308B1/pt not_active IP Right Cessation
- 1999-03-30 AT AT99913557T patent/ATE309335T1/de not_active IP Right Cessation
- 1999-03-30 JP JP2000542438A patent/JP4364433B2/ja not_active Expired - Lifetime
- 1999-03-31 TW TW088105128A patent/TW581812B/zh not_active IP Right Cessation
- 1999-03-31 AR ARP990101492A patent/AR014811A1/es not_active Application Discontinuation
-
2000
- 2000-09-28 IL IL138746A patent/IL138746A/en not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| CA2324380C (en) | 2009-02-24 |
| ATE309335T1 (de) | 2005-11-15 |
| BR9909308A (pt) | 2001-10-02 |
| HK1030966A1 (en) | 2001-05-25 |
| WO1999051725A2 (en) | 1999-10-14 |
| CN1300320A (zh) | 2001-06-20 |
| EP1068303A2 (en) | 2001-01-17 |
| DE69928236D1 (de) | 2005-12-15 |
| JP2002510712A (ja) | 2002-04-09 |
| WO1999051725A3 (en) | 1999-12-02 |
| AU3165599A (en) | 1999-10-25 |
| BR9909308B1 (pt) | 2010-11-30 |
| EP1068303B1 (en) | 2005-11-09 |
| JP4364433B2 (ja) | 2009-11-18 |
| IL138746A (en) | 2006-12-10 |
| US7098304B1 (en) | 2006-08-29 |
| CA2324380A1 (en) | 1999-10-14 |
| AR014811A1 (es) | 2001-03-28 |
| CN1171995C (zh) | 2004-10-20 |
| DE69928236T2 (de) | 2006-08-03 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| HUE026699T2 (en) | Peptides and their applications from the major allergen of ragweed (Ambrosia artemisiifolia) | |
| CN106967696A (zh) | 一种蒿属植物花粉的过敏原及其应用 | |
| US5457029A (en) | Nuclear antigen La | |
| DK2588495T3 (en) | Histoncitrullinerede peptides and uses thereof | |
| AU2006246342B2 (en) | Melanoma-associated endogenous retrovirus (MERV) derived peptide sequences and their therapeutic/ diagnostic use | |
| JP5377288B2 (ja) | 慢性関節リウマチの治療に有用な、マクロファージの活性を調整するペプチド | |
| TW581812B (en) | Assay for the diagnosis of schizophrenia based on a new peptide | |
| JP3220451B2 (ja) | ブタクサからのアレルゲン蛋白質およびそれらの使用 | |
| EP3294901B1 (en) | Autoantigens for diagnosis of rheumatoid arthritis | |
| KAUPPINEN et al. | Mutant derivatives of the main respiratory allergen of cow are less allergenic than the intact molecule | |
| Youinou et al. | The antiperinuclear factor and antikeratin antibody systems | |
| CN108948153B (zh) | 一种瓜氨酸修饰肽抗原组合及其应用 | |
| CN108948173B (zh) | 一种瓜氨酸修饰肽及其应用 | |
| US5407833A (en) | Peptides of the SM-D antigen and their use for diagnosis of systemic lupus erythematosus | |
| Huguet et al. | Identification by proteomic tool of atypical anti‐liver/kidney microsome autoantibodies targets in de novo autoimmune hepatitis after liver transplantation | |
| KR101419791B1 (ko) | 쯔쯔가무시 균 특이 항체를 검출하기 위한 조성물 및 키트 | |
| CN105001342A (zh) | 一种重组人自身抗原SSB-La | |
| Youinou et al. | Anti-Ro (SSA) and anti-La (SSB) antibodies in autoimmune rheumatic diseases | |
| CN108948174B (zh) | 一种瓜氨酸修饰肽及其应用 | |
| WO2004087747A2 (en) | Citrullinated synthetic peptides and uses thereof | |
| JP5048205B2 (ja) | 精神分裂病の診断のための新規ペプチド | |
| US20060211056A1 (en) | Leishmania antigens suitable for a diagnostic kit of Leishmania | |
| CN101906420B (zh) | 人聚角微丝蛋白基因原核表达系统及其表达蛋白的应用 | |
| CN105001341A (zh) | 一种重组人自身抗原JoSmD1 | |
| JP2025104819A (ja) | 特定の遺伝子型を有するｈｌａに結合するエピトープの特定方法 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM4A | Annulment or lapse of patent due to non-payment of fees |