CA2127550A1 - Proteine de surface streptococcique multifonctionnelle - Google Patents
Proteine de surface streptococcique multifonctionnelleInfo
- Publication number
- CA2127550A1 CA2127550A1 CA002127550A CA2127550A CA2127550A1 CA 2127550 A1 CA2127550 A1 CA 2127550A1 CA 002127550 A CA002127550 A CA 002127550A CA 2127550 A CA2127550 A CA 2127550A CA 2127550 A1 CA2127550 A1 CA 2127550A1
- Authority
- CA
- Canada
- Prior art keywords
- sdh
- activity
- protein
- streptococci
- adp
- Prior art date
- 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.)
- Abandoned
Links
- 102000018697 Membrane Proteins Human genes 0.000 title abstract description 7
- 108010052285 Membrane Proteins Proteins 0.000 title abstract description 7
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 claims abstract description 44
- 230000000694 effects Effects 0.000 claims abstract description 41
- 230000027455 binding Effects 0.000 claims abstract description 29
- 102000016359 Fibronectins Human genes 0.000 claims abstract description 15
- 108010067306 Fibronectins Proteins 0.000 claims abstract description 15
- 108010014251 Muramidase Proteins 0.000 claims abstract description 11
- 102000016943 Muramidase Human genes 0.000 claims abstract description 11
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims abstract description 11
- 229960000274 lysozyme Drugs 0.000 claims abstract description 11
- 239000004325 lysozyme Substances 0.000 claims abstract description 11
- 235000010335 lysozyme Nutrition 0.000 claims abstract description 11
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 claims abstract description 8
- 229960005486 vaccine Drugs 0.000 claims abstract description 6
- 102000009062 ADP Ribose Transferases Human genes 0.000 claims abstract 5
- 108010049290 ADP Ribose Transferases Proteins 0.000 claims abstract 5
- 108090000623 proteins and genes Proteins 0.000 claims description 93
- 102000004169 proteins and genes Human genes 0.000 claims description 89
- 238000000034 method Methods 0.000 claims description 31
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 21
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 20
- 239000000203 mixture Substances 0.000 claims description 13
- 101710088194 Dehydrogenase Proteins 0.000 claims description 11
- 230000005764 inhibitory process Effects 0.000 claims description 4
- 210000004400 mucous membrane Anatomy 0.000 claims description 3
- 230000003381 solubilizing effect Effects 0.000 claims description 2
- 108010020056 Hydrogenase Proteins 0.000 claims 3
- 241000124008 Mammalia Species 0.000 claims 2
- 239000003937 drug carrier Substances 0.000 claims 1
- 238000002360 preparation method Methods 0.000 abstract description 4
- 206010061372 Streptococcal infection Diseases 0.000 abstract description 3
- 235000018102 proteins Nutrition 0.000 description 84
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 36
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 description 21
- 229950006238 nadide Drugs 0.000 description 21
- 239000000872 buffer Substances 0.000 description 19
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
- 241000894006 Bacteria Species 0.000 description 15
- 239000000499 gel Substances 0.000 description 15
- 102000004190 Enzymes Human genes 0.000 description 14
- 108090000790 Enzymes Proteins 0.000 description 14
- 229940088598 enzyme Drugs 0.000 description 14
- 239000000284 extract Substances 0.000 description 14
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 14
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 14
- 238000006243 chemical reaction Methods 0.000 description 13
- 150000002500 ions Chemical class 0.000 description 13
- 238000004458 analytical method Methods 0.000 description 12
- 235000001014 amino acid Nutrition 0.000 description 10
- 238000001262 western blot Methods 0.000 description 10
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 9
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
- 241000283973 Oryctolagus cuniculus Species 0.000 description 9
- 239000002253 acid Substances 0.000 description 9
- 150000001413 amino acids Chemical class 0.000 description 9
- 210000004379 membrane Anatomy 0.000 description 9
- 239000012528 membrane Substances 0.000 description 9
- 239000011734 sodium Substances 0.000 description 9
- 238000002965 ELISA Methods 0.000 description 8
- 241000282414 Homo sapiens Species 0.000 description 8
- 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 8
- 108060008487 Myosin Proteins 0.000 description 8
- 102000003505 Myosin Human genes 0.000 description 8
- 230000001580 bacterial effect Effects 0.000 description 8
- 229910052708 sodium Inorganic materials 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- 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 7
- 239000007983 Tris buffer Substances 0.000 description 7
- 102000004142 Trypsin Human genes 0.000 description 7
- 108090000631 Trypsin Proteins 0.000 description 7
- 210000002421 cell wall Anatomy 0.000 description 7
- 239000002244 precipitate Substances 0.000 description 7
- 108090000765 processed proteins & peptides Proteins 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 7
- 239000012588 trypsin Substances 0.000 description 7
- 230000002255 enzymatic effect Effects 0.000 description 6
- 238000000605 extraction Methods 0.000 description 6
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 6
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 6
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 6
- 230000005730 ADP ribosylation Effects 0.000 description 5
- 102000007469 Actins Human genes 0.000 description 5
- 108010085238 Actins Proteins 0.000 description 5
- 229910019142 PO4 Inorganic materials 0.000 description 5
- 239000002033 PVDF binder Substances 0.000 description 5
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 239000010452 phosphate Substances 0.000 description 5
- 102000004196 processed proteins & peptides Human genes 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 238000011282 treatment Methods 0.000 description 5
- LXJXRIRHZLFYRP-VKHMYHEASA-N D-glyceraldehyde 3-phosphate Chemical compound O=C[C@H](O)COP(O)(O)=O LXJXRIRHZLFYRP-VKHMYHEASA-N 0.000 description 4
- MWUXSHHQAYIFBG-UHFFFAOYSA-N Nitric oxide Chemical compound O=[N] MWUXSHHQAYIFBG-UHFFFAOYSA-N 0.000 description 4
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 4
- 125000003275 alpha amino acid group Chemical group 0.000 description 4
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 4
- 235000011130 ammonium sulphate Nutrition 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 238000003795 desorption Methods 0.000 description 4
- 210000003743 erythrocyte Anatomy 0.000 description 4
- 239000008188 pellet Substances 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- LXJXRIRHZLFYRP-VKHMYHEASA-L (R)-2-Hydroxy-3-(phosphonooxy)-propanal Natural products O=C[C@H](O)COP([O-])([O-])=O LXJXRIRHZLFYRP-VKHMYHEASA-L 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 241001024304 Mino Species 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- 241000194017 Streptococcus Species 0.000 description 3
- PWJFNRJRHXWEPT-AOOZFPJJSA-N [[(2r,3s,4r,5r)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2r,3r,4r)-2,3,4-trihydroxy-5-oxopentyl] hydrogen phosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OC[C@@H](O)[C@@H](O)[C@@H](O)C=O)[C@@H](O)[C@H]1O PWJFNRJRHXWEPT-AOOZFPJJSA-N 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 150000007513 acids Chemical class 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 210000004027 cell Anatomy 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 210000004877 mucosa Anatomy 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
- 229940012957 plasmin Drugs 0.000 description 3
- 230000009257 reactivity Effects 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 239000007790 solid phase Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 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 2
- 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 2
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 2
- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- 102000002322 Egg Proteins Human genes 0.000 description 2
- 108010000912 Egg Proteins Proteins 0.000 description 2
- 101001061354 Gallus gallus Glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 2
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 2
- 239000007995 HEPES buffer Substances 0.000 description 2
- 101710085938 Matrix protein Proteins 0.000 description 2
- 101710127721 Membrane protein Proteins 0.000 description 2
- 108010034119 Myosin Subfragments Proteins 0.000 description 2
- MUPFEKGTMRGPLJ-RMMQSMQOSA-N Raffinose Natural products O(C[C@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O[C@@]2(CO)[C@H](O)[C@@H](O)[C@@H](CO)O2)O1)[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 MUPFEKGTMRGPLJ-RMMQSMQOSA-N 0.000 description 2
- 229920005654 Sephadex Polymers 0.000 description 2
- 239000012507 Sephadex™ Substances 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- 241001505901 Streptococcus sp. 'group A' Species 0.000 description 2
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 2
- 102000005937 Tropomyosin Human genes 0.000 description 2
- 108010030743 Tropomyosin Proteins 0.000 description 2
- MUPFEKGTMRGPLJ-UHFFFAOYSA-N UNPD196149 Natural products OC1C(O)C(CO)OC1(CO)OC1C(O)C(O)C(O)C(COC2C(C(O)C(O)C(CO)O2)O)O1 MUPFEKGTMRGPLJ-UHFFFAOYSA-N 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 150000001299 aldehydes Chemical class 0.000 description 2
- 238000000376 autoradiography Methods 0.000 description 2
- 230000008033 biological extinction Effects 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 230000002860 competitive effect Effects 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 230000001086 cytosolic effect Effects 0.000 description 2
- -1 dioxetane anion Chemical class 0.000 description 2
- 229910000397 disodium phosphate Inorganic materials 0.000 description 2
- 235000014103 egg white Nutrition 0.000 description 2
- 210000000969 egg white Anatomy 0.000 description 2
- 235000013601 eggs Nutrition 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 238000012933 kinetic analysis Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 210000003205 muscle Anatomy 0.000 description 2
- YFCUZWYIPBUQBD-ZOWNYOTGSA-N n-[(3s)-7-amino-1-chloro-2-oxoheptan-3-yl]-4-methylbenzenesulfonamide;hydron;chloride Chemical compound Cl.CC1=CC=C(S(=O)(=O)N[C@@H](CCCCN)C(=O)CCl)C=C1 YFCUZWYIPBUQBD-ZOWNYOTGSA-N 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- MUPFEKGTMRGPLJ-ZQSKZDJDSA-N raffinose 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[C@@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)O1 MUPFEKGTMRGPLJ-ZQSKZDJDSA-N 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 210000002027 skeletal muscle Anatomy 0.000 description 2
- 238000004611 spectroscopical analysis Methods 0.000 description 2
- 108010010318 streptococcal M protein Proteins 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- 239000003643 water by type Substances 0.000 description 2
- NNJPGOLRFBJNIW-HNNXBMFYSA-N (-)-demecolcine Chemical compound C1=C(OC)C(=O)C=C2[C@@H](NC)CCC3=CC(OC)=C(OC)C(OC)=C3C2=C1 NNJPGOLRFBJNIW-HNNXBMFYSA-N 0.000 description 1
- BHMLFPOTZYRDKA-IRXDYDNUSA-N (2s)-2-[(s)-(2-iodophenoxy)-phenylmethyl]morpholine Chemical compound IC1=CC=CC=C1O[C@@H](C=1C=CC=CC=1)[C@H]1OCCNC1 BHMLFPOTZYRDKA-IRXDYDNUSA-N 0.000 description 1
- NNRFRJQMBSBXGO-CIUDSAMLSA-N (3s)-3-[[2-[[(2s)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]acetyl]amino]-4-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-oxobutanoic acid Chemical compound NC(N)=NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(O)=O NNRFRJQMBSBXGO-CIUDSAMLSA-N 0.000 description 1
- IEQAICDLOKRSRL-UHFFFAOYSA-N 2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-(2-dodecoxyethoxy)ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethanol Chemical compound CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO IEQAICDLOKRSRL-UHFFFAOYSA-N 0.000 description 1
- 125000000954 2-hydroxyethyl group Chemical group [H]C([*])([H])C([H])([H])O[H] 0.000 description 1
- LJQLQCAXBUHEAZ-UWTATZPHSA-N 3-phospho-D-glyceroyl dihydrogen phosphate Chemical compound OP(=O)(O)OC[C@@H](O)C(=O)OP(O)(O)=O LJQLQCAXBUHEAZ-UWTATZPHSA-N 0.000 description 1
- BDDLHHRCDSJVKV-UHFFFAOYSA-N 7028-40-2 Chemical compound CC(O)=O.CC(O)=O.CC(O)=O.CC(O)=O BDDLHHRCDSJVKV-UHFFFAOYSA-N 0.000 description 1
- SRNWOUGRCWSEMX-TYASJMOZSA-N ADP-D-ribose Chemical compound C([C@H]1O[C@H]([C@@H]([C@@H]1O)O)N1C=2N=CN=C(C=2N=C1)N)OP(O)(=O)OP(O)(=O)OC[C@H]1OC(O)[C@H](O)[C@@H]1O SRNWOUGRCWSEMX-TYASJMOZSA-N 0.000 description 1
- 102000020236 ADP-ribosylarginine hydrolase Human genes 0.000 description 1
- 108010079768 ADP-ribosylarginine hydrolase Proteins 0.000 description 1
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 1
- 108700023418 Amidases Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 101150058765 BACE1 gene Proteins 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- KXDHJXZQYSOELW-UHFFFAOYSA-M Carbamate Chemical compound NC([O-])=O KXDHJXZQYSOELW-UHFFFAOYSA-M 0.000 description 1
- 241000283153 Cetacea Species 0.000 description 1
- QDHHCQZDFGDHMP-UHFFFAOYSA-N Chloramine Chemical compound ClN QDHHCQZDFGDHMP-UHFFFAOYSA-N 0.000 description 1
- 206010008631 Cholera Diseases 0.000 description 1
- 241000511343 Chondrostoma nasus Species 0.000 description 1
- 241000543381 Cliftonia monophylla Species 0.000 description 1
- 101100129080 Crassostrea virginica lysoz1 gene Proteins 0.000 description 1
- 102000010831 Cytoskeletal Proteins Human genes 0.000 description 1
- 108010037414 Cytoskeletal Proteins Proteins 0.000 description 1
- MNQZXJOMYWMBOU-VKHMYHEASA-N D-glyceraldehyde Chemical compound OC[C@@H](O)C=O MNQZXJOMYWMBOU-VKHMYHEASA-N 0.000 description 1
- 125000000824 D-ribofuranosyl group Chemical group [H]OC([H])([H])[C@@]1([H])OC([H])(*)[C@]([H])(O[H])[C@]1([H])O[H] 0.000 description 1
- BVTJGGGYKAMDBN-UHFFFAOYSA-N Dioxetane Chemical compound C1COO1 BVTJGGGYKAMDBN-UHFFFAOYSA-N 0.000 description 1
- 241000698776 Duma Species 0.000 description 1
- 101150039033 Eci2 gene Proteins 0.000 description 1
- 241001517310 Eria Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 240000001973 Ficus microcarpa Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- OVSKVOOUFAKODB-UWVGGRQHSA-N Gly-Arg-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)CN)CCCN=C(N)N OVSKVOOUFAKODB-UWVGGRQHSA-N 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101001018100 Homo sapiens Lysozyme C Proteins 0.000 description 1
- 101000829980 Homo sapiens Ral guanine nucleotide dissociation stimulator Proteins 0.000 description 1
- 241001527806 Iti Species 0.000 description 1
- 241001459757 Juga Species 0.000 description 1
- 235000019766 L-Lysine Nutrition 0.000 description 1
- 125000000570 L-alpha-aspartyl group Chemical group [H]OC(=O)C([H])([H])[C@]([H])(N([H])[H])C(*)=O 0.000 description 1
- 125000000899 L-alpha-glutamyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C([H])([H])C(O[H])=O 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- 102000008192 Lactoglobulins Human genes 0.000 description 1
- 108010060630 Lactoglobulins Proteins 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- HOKDBMAJZXIPGC-UHFFFAOYSA-N Mequitazine Chemical compound C12=CC=CC=C2SC2=CC=CC=C2N1CC1C(CC2)CCN2C1 HOKDBMAJZXIPGC-UHFFFAOYSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000357437 Mola Species 0.000 description 1
- SOWBFZRMHSNYGE-UHFFFAOYSA-N Monoamide-Oxalic acid Natural products NC(=O)C(O)=O SOWBFZRMHSNYGE-UHFFFAOYSA-N 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 102100026933 Myelin-associated neurite-outgrowth inhibitor Human genes 0.000 description 1
- BAWFJGJZGIEFAR-NNYOXOHSSA-O NAD(+) Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-O 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- KQHKSGRIBYJYFX-UHFFFAOYSA-J Ponceau S Chemical compound [Na+].[Na+].[Na+].[Na+].Oc1c(cc2cc(ccc2c1N=Nc1ccc(cc1S([O-])(=O)=O)N=Nc1ccc(cc1)S([O-])(=O)=O)S([O-])(=O)=O)S([O-])(=O)=O KQHKSGRIBYJYFX-UHFFFAOYSA-J 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 102100023320 Ral guanine nucleotide dissociation stimulator Human genes 0.000 description 1
- 101100014660 Rattus norvegicus Gimap8 gene Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 240000002407 Solanum quitoense Species 0.000 description 1
- 241000194026 Streptococcus gordonii Species 0.000 description 1
- 241000193996 Streptococcus pyogenes Species 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- WFWLQNSHRPWKFK-UHFFFAOYSA-N Tegafur Chemical compound O=C1NC(=O)C(F)=CN1C1OCCC1 WFWLQNSHRPWKFK-UHFFFAOYSA-N 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- XJLXINKUBYWONI-DQQFMEOOSA-N [[(2r,3r,4r,5r)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2s,3r,4s,5s)-5-(3-carbamoylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate Chemical compound NC(=O)C1=CC=C[N+]([C@@H]2[C@H]([C@@H](O)[C@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-DQQFMEOOSA-N 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- VREFGVBLTWBCJP-UHFFFAOYSA-N alprazolam Chemical compound C12=CC(Cl)=CC=C2N2C(C)=NN=C2CN=C1C1=CC=CC=C1 VREFGVBLTWBCJP-UHFFFAOYSA-N 0.000 description 1
- 102000005922 amidase Human genes 0.000 description 1
- 238000003277 amino acid sequence analysis Methods 0.000 description 1
- 239000001166 ammonium sulphate Substances 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 238000000211 autoradiogram Methods 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 102000023732 binding proteins Human genes 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000002759 chromosomal effect Effects 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000003436 cytoskeletal effect Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000010217 densitometric analysis Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- XEYBHCRIKKKOSS-UHFFFAOYSA-N disodium;azanylidyneoxidanium;iron(2+);pentacyanide Chemical compound [Na+].[Na+].[Fe+2].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-].[O+]#N XEYBHCRIKKKOSS-UHFFFAOYSA-N 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- MOTZDAYCYVMXPC-UHFFFAOYSA-N dodecyl hydrogen sulfate Chemical compound CCCCCCCCCCCCOS(O)(=O)=O MOTZDAYCYVMXPC-UHFFFAOYSA-N 0.000 description 1
- 229940043264 dodecyl sulfate Drugs 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 108091005594 ethylated proteins Proteins 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- MNQZXJOMYWMBOU-UHFFFAOYSA-N glyceraldehyde Chemical compound OCC(O)C=O MNQZXJOMYWMBOU-UHFFFAOYSA-N 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000005802 health problem Effects 0.000 description 1
- 230000002949 hemolytic effect Effects 0.000 description 1
- 235000011167 hydrochloric acid Nutrition 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- ATADHKWKHYVBTJ-UHFFFAOYSA-N hydron;4-[1-hydroxy-2-(methylamino)ethyl]benzene-1,2-diol;chloride Chemical compound Cl.CNCC(O)C1=CC=C(O)C(O)=C1 ATADHKWKHYVBTJ-UHFFFAOYSA-N 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 210000004201 immune sera Anatomy 0.000 description 1
- 229940042743 immune sera Drugs 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 239000011630 iodine Substances 0.000 description 1
- PNDPGZBMCMUPRI-UHFFFAOYSA-N iodine Chemical compound II PNDPGZBMCMUPRI-UHFFFAOYSA-N 0.000 description 1
- 229910052740 iodine Inorganic materials 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 101150091003 lysoz gene Proteins 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 108091005592 methylated proteins Proteins 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 150000007522 mineralic acids Chemical class 0.000 description 1
- 230000010807 negative regulation of binding Effects 0.000 description 1
- PMQNLFGGVGXOSM-QRQUECDASA-N nff 2 Chemical compound C([C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CCC)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCNC=1C(=CC(=CC=1)[N+]([O-])=O)[N+]([O-])=O)C(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)C(CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCNC(N)=N)NC(=O)CC=1C=2C=CC(OC)=CC=2OC(=O)C=1)C1=CC=C(O)C=C1 PMQNLFGGVGXOSM-QRQUECDASA-N 0.000 description 1
- 125000000449 nitro group Chemical group [O-][N+](*)=O 0.000 description 1
- 230000014207 opsonization Effects 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 108010031256 phosducin Proteins 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000223 polyglycerol Polymers 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 239000013014 purified material Substances 0.000 description 1
- 150000003222 pyridines Chemical class 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 102220037654 rs587780327 Human genes 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 229920006298 saran Polymers 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 230000000405 serological effect Effects 0.000 description 1
- 238000007873 sieving Methods 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 229940083618 sodium nitroprusside Drugs 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 239000011877 solvent mixture Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- OBTWBSRJZRCYQV-UHFFFAOYSA-N sulfuryl difluoride Chemical compound FS(F)(=O)=O OBTWBSRJZRCYQV-UHFFFAOYSA-N 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 230000036962 time dependent Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 239000002753 trypsin inhibitor Substances 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0008—Oxidoreductases (1.) acting on the aldehyde or oxo group of donors (1.2)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/315—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Streptococcus (G), e.g. Enterococci
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y102/00—Oxidoreductases acting on the aldehyde or oxo group of donors (1.2)
- C12Y102/01—Oxidoreductases acting on the aldehyde or oxo group of donors (1.2) with NAD+ or NADP+ as acceptor (1.2.1)
- C12Y102/01009—Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (1.2.1.9)
-
- 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
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- General Chemical & Material Sciences (AREA)
- Biotechnology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US81817092A | 1992-01-08 | 1992-01-08 | |
| US07/818,170 | 1992-01-08 | ||
| US91373292A | 1992-07-15 | 1992-07-15 | |
| US07/913,732 | 1992-07-15 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2127550A1 true CA2127550A1 (fr) | 1993-07-22 |
Family
ID=27124235
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002127550A Abandoned CA2127550A1 (fr) | 1992-01-08 | 1993-01-07 | Proteine de surface streptococcique multifonctionnelle |
Country Status (5)
| Country | Link |
|---|---|
| EP (1) | EP0672123A1 (fr) |
| JP (1) | JPH07502896A (fr) |
| AU (1) | AU668908B2 (fr) |
| CA (1) | CA2127550A1 (fr) |
| WO (1) | WO1993014198A1 (fr) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5928900A (en) * | 1993-09-01 | 1999-07-27 | The Rockefeller University | Bacterial exported proteins and acellular vaccines based thereon |
| TW448185B (en) * | 1993-11-05 | 2001-08-01 | Lilly Co Eli | Vaccine design and production |
| US6355255B1 (en) | 1998-12-07 | 2002-03-12 | Regents Of The University Of Minnesota | Streptococcal C5a peptidase vaccine |
| US5846547A (en) * | 1996-01-22 | 1998-12-08 | Regents Of The University Of Minnesota | Streptococcal C5a peptidase vaccine |
| US6245335B1 (en) | 1996-05-01 | 2001-06-12 | The Rockefeller University | Choline binding proteins for anti-pneumococcal vaccines |
| WO2000037646A2 (fr) | 1998-12-22 | 2000-06-29 | Microscience Limited | Genes, proteines, et leur utilisation |
| CA2354843A1 (fr) * | 1998-12-22 | 2000-06-29 | Microscience Limited | Proteines de surface exterieure, leurs genes, et leur utilisation |
| US6890539B2 (en) | 1998-12-22 | 2005-05-10 | Microscience, Ltd. | Genes and proteins, and their use |
| US7256265B2 (en) | 1999-12-03 | 2007-08-14 | Regents Of The University Of Minnesota | Streptococcal C5a peptidase vaccine |
| DK1294771T3 (da) | 2000-06-12 | 2008-12-15 | Univ Saskatchewan | Kimært GapC-protein fra Streptococcus og anvendelse deraf til vaccinering og diagnosticering |
| ES2648231T3 (es) | 2008-11-05 | 2017-12-29 | Wyeth Llc | Composición inmunogénica de múltiples componentes para la prevención de la enfermedad por estreptococos beta hemolíticos (EBH) |
| CN111198271B (zh) * | 2018-11-16 | 2023-04-28 | 山东泽济生物科技有限公司 | 一种用于甘油醛-3-磷酸脱氢酶检测的化学发光酶联免疫试剂盒 |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2199932T3 (es) * | 1989-06-21 | 2004-03-01 | The Rockefeller University | Poxvirus recombinante y vacuna estreptococica que contiene proteina m. |
-
1993
- 1993-01-07 EP EP93902960A patent/EP0672123A1/fr not_active Withdrawn
- 1993-01-07 CA CA002127550A patent/CA2127550A1/fr not_active Abandoned
- 1993-01-07 JP JP5512544A patent/JPH07502896A/ja active Pending
- 1993-01-07 WO PCT/US1993/000082 patent/WO1993014198A1/fr not_active Application Discontinuation
- 1993-01-07 AU AU34351/93A patent/AU668908B2/en not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| JPH07502896A (ja) | 1995-03-30 |
| WO1993014198A1 (fr) | 1993-07-22 |
| EP0672123A1 (fr) | 1995-09-20 |
| AU668908B2 (en) | 1996-05-23 |
| AU3435193A (en) | 1993-08-03 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Lu et al. | Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence similarity and antigenic cross-reactivity with their hornet and wasp homologs and possible implications for clinical allergy | |
| Clark et al. | Identification and isolation of a mammalian protein which is antigenically and functionally related to the phospholipase A2 stimulatory peptide melittin. | |
| Bohnsack et al. | Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus | |
| JP3816515B2 (ja) | ホスホリパーゼ及びヒアルロニダーゼのようなスズメバチ毒酵素のクローニング及び組換え体の生産並びにそれに基づく免疫学的治療 | |
| CA2127550A1 (fr) | Proteine de surface streptococcique multifonctionnelle | |
| JP3976334B2 (ja) | Ｂ群れんさ球菌の多くの菌株に対する免疫を与える細胞表面タンパク質であるタンパク質Ｒｉｂ、そのタンパク質の精製方法、薬剤キットおよび医薬組成物 | |
| Buchanan et al. | Activation of the cell wall degrading protease, lysin, during sexual signalling in Chlamydomonas: the enzyme is stored as an inactive, higher relative molecular mass precursor in the periplasm. | |
| Allis et al. | A conserved histone variant enriched in nucleoli of mammalian cells | |
| Kaslow et al. | Alkylation of Cysteine 41, but Not Cysteine 200, Decreases the ADP-ribosytransferase Activity of the S1 Subunit of Pertussis Toxin | |
| Brunisholz et al. | The membrane location of the B890-complex from Rhodospirillum rubrum and the effect of carotenoid on the conformation of its two apoproteins exposed at the cytoplasmic surface | |
| JPH0193537A (ja) | アンギオゲニンの抑制剤 | |
| Schleicher et al. | Isolation and characterization of calmodulin from the motile green alga Chlamydomonas reinhardtii | |
| EP0463059A1 (fr) | Proteines allergenes tirees de l'ambrosie et utilisations de ces proteines | |
| US5698204A (en) | Recombinant allergenic proteins from ragweed pollen | |
| Casais et al. | Hypoderma lineatum: Expression of Enzymatically Active Hypodermin C inEscherichia coliand Its Use for the Immunodiagnosis of Hypodermosis | |
| Rivas et al. | Biochemical characterization of the protective membrane glycoprotein GP46/M-2 of Leishmania amazonensis | |
| US5367063A (en) | Human phospholipase activating protein and methods for diagnosis of rheumatoid arthritis | |
| CZ20033430A3 (cs) | Gen spojený s virulencí parasitů Leishmanie | |
| US5202426A (en) | Eucaryotic NAD cyclases | |
| Li et al. | Cancer-associated lactate dehydrogenase is a tyrosylphosphorylated form of human LDH-A, skeletal muscle isoenzyme | |
| US5831074A (en) | Eucaryotic NAD cyclases | |
| Rikiishi et al. | Superantigenicity of helper T‐cell mitogen (SPM‐2) isolated from culture supernatants of Streptococcus pyogenes | |
| YAMASHITA | Immunohistochemical study of amylase and deoxyribonuclease in rat parotid gland | |
| EP2110436B1 (fr) | Polypeptides dotés d'une activité de stimulation des neutrophiles | |
| JPH05506239A (ja) | Ｔ細胞抑制蛋白質 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued | ||
| FZDE | Discontinued |
Effective date: 20000107 |