FI94051C - Proteinfragment av Pectinatus-bakterier - Google Patents
Proteinfragment av Pectinatus-bakterier Download PDFInfo
- Publication number
- FI94051C FI94051C FI924835A FI924835A FI94051C FI 94051 C FI94051 C FI 94051C FI 924835 A FI924835 A FI 924835A FI 924835 A FI924835 A FI 924835A FI 94051 C FI94051 C FI 94051C
- Authority
- FI
- Finland
- Prior art keywords
- ala
- asn
- vai
- pectinatus
- ser
- Prior art date
Links
- 241000606012 Pectinatus Species 0.000 title claims description 24
- 239000012634 fragment Substances 0.000 title claims description 7
- 108010077805 Bacterial Proteins Proteins 0.000 title description 2
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 29
- 108090000623 proteins and genes Proteins 0.000 claims description 25
- 102000004169 proteins and genes Human genes 0.000 claims description 24
- 230000000890 antigenic effect Effects 0.000 claims description 17
- ABHIXYDMILIUKV-CIUDSAMLSA-N Lys-Asn-Asn Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O ABHIXYDMILIUKV-CIUDSAMLSA-N 0.000 claims description 8
- AAQGRPOPTAUUBM-ZLUOBGJFSA-N Ala-Ala-Asn Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(O)=O AAQGRPOPTAUUBM-ZLUOBGJFSA-N 0.000 claims description 7
- APKRGYLBSCWJJP-FXQIFTODSA-N Pro-Ala-Asp Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](C)C(=O)N[C@@H](CC(O)=O)C(O)=O APKRGYLBSCWJJP-FXQIFTODSA-N 0.000 claims description 7
- GFHXZNVJIKMAGO-IHRRRGAJSA-N Pro-Phe-Ser Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CO)C(O)=O GFHXZNVJIKMAGO-IHRRRGAJSA-N 0.000 claims description 7
- HHJFMHQYEAAOBM-ZLUOBGJFSA-N Ser-Ser-Ala Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(O)=O HHJFMHQYEAAOBM-ZLUOBGJFSA-N 0.000 claims description 7
- 108010077245 asparaginyl-proline Proteins 0.000 claims description 7
- FIJMQLGQLBLBOL-HJGDQZAQSA-N Leu-Asn-Thr Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O FIJMQLGQLBLBOL-HJGDQZAQSA-N 0.000 claims description 5
- 238000000034 method Methods 0.000 claims description 5
- 239000002344 surface layer Substances 0.000 claims description 5
- CIDICGYKRUTYLE-FXQIFTODSA-N Met-Ser-Ala Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(O)=O CIDICGYKRUTYLE-FXQIFTODSA-N 0.000 claims description 4
- 230000003053 immunization Effects 0.000 claims description 3
- 238000002649 immunization Methods 0.000 claims description 3
- 230000001268 conjugating effect Effects 0.000 claims description 2
- 235000018102 proteins Nutrition 0.000 description 23
- 102000004196 processed proteins & peptides Human genes 0.000 description 16
- 150000001413 amino acids Chemical class 0.000 description 13
- 235000001014 amino acid Nutrition 0.000 description 11
- 229940024606 amino acid Drugs 0.000 description 11
- 239000000427 antigen Substances 0.000 description 9
- 108091007433 antigens Proteins 0.000 description 9
- 102000036639 antigens Human genes 0.000 description 9
- 210000004027 cell Anatomy 0.000 description 8
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 7
- 239000012528 membrane Substances 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 241000894006 Bacteria Species 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
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000000284 extract Substances 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 2
- YHOPXCAOTRUGLV-XAMCCFCMSA-N Ala-Ala-Asp-Asp Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O YHOPXCAOTRUGLV-XAMCCFCMSA-N 0.000 description 2
- HHRAXZAYZFFRAM-CIUDSAMLSA-N Ala-Leu-Asn Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O HHRAXZAYZFFRAM-CIUDSAMLSA-N 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-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
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 241000008319 Pectinatus cerevisiiphilus Species 0.000 description 2
- 101800005149 Peptide B Proteins 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- XUDRHBPSPAPDJP-SRVKXCTJSA-N Ser-Lys-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CO XUDRHBPSPAPDJP-SRVKXCTJSA-N 0.000 description 2
- IMDMLDSVUSMAEJ-HJGDQZAQSA-N Thr-Leu-Asn Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O IMDMLDSVUSMAEJ-HJGDQZAQSA-N 0.000 description 2
- QPMSXSBEVQLBIL-CZRHPSIPSA-N ac1mix0p Chemical compound C1=CC=C2N(C[C@H](C)CN(C)C)C3=CC(OC)=CC=C3SC2=C1.O([C@H]1[C@]2(OC)C=CC34C[C@@H]2[C@](C)(O)CCC)C2=C5[C@]41CCN(C)[C@@H]3CC5=CC=C2O QPMSXSBEVQLBIL-CZRHPSIPSA-N 0.000 description 2
- 108010070783 alanyltyrosine Proteins 0.000 description 2
- 235000013405 beer Nutrition 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 238000011109 contamination Methods 0.000 description 2
- 239000013256 coordination polymer 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
- 238000001514 detection method Methods 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 210000004898 n-terminal fragment Anatomy 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 230000003389 potentiating effect Effects 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 239000000523 sample Substances 0.000 description 2
- 108010048397 seryl-lysyl-leucine Proteins 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- 241000024188 Andala Species 0.000 description 1
- APHUDFFMXFYRKP-CIUDSAMLSA-N Asn-Asn-Lys Chemical compound C(CCN)C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)N)NC(=O)[C@H](CC(=O)N)N APHUDFFMXFYRKP-CIUDSAMLSA-N 0.000 description 1
- PNHQRQTVBRDIEF-CIUDSAMLSA-N Asn-Leu-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)N)N PNHQRQTVBRDIEF-CIUDSAMLSA-N 0.000 description 1
- KEUNWIXNKVWCFL-FXQIFTODSA-N Asn-Met-Ser Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CO)C(O)=O KEUNWIXNKVWCFL-FXQIFTODSA-N 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- NPAYJTAXWXJKLO-NAKRPEOUSA-N Ile-Met-Ser Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CO)C(=O)O)N NPAYJTAXWXJKLO-NAKRPEOUSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- OXKYZSRZKBTVEY-ZPFDUUQYSA-N Leu-Asn-Ile Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O OXKYZSRZKBTVEY-ZPFDUUQYSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- FACUGMGEFUEBTI-SRVKXCTJSA-N Lys-Asn-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)CCCCN FACUGMGEFUEBTI-SRVKXCTJSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- DSZFTPCSFVWMKP-DCAQKATOSA-N Met-Ser-Lys Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCCCN DSZFTPCSFVWMKP-DCAQKATOSA-N 0.000 description 1
- VCUFZILGIRCDQQ-KRWDZBQOSA-N N-[[(5S)-2-oxo-3-(2-oxo-3H-1,3-benzoxazol-6-yl)-1,3-oxazolidin-5-yl]methyl]-2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidine-5-carboxamide Chemical compound O=C1O[C@H](CN1C1=CC2=C(NC(O2)=O)C=C1)CNC(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F VCUFZILGIRCDQQ-KRWDZBQOSA-N 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 101710099182 S-layer protein Proteins 0.000 description 1
- VIIJCAQMJBHSJH-FXQIFTODSA-N Ser-Met-Ser Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CO)C(O)=O VIIJCAQMJBHSJH-FXQIFTODSA-N 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 102100021941 Sorcin Human genes 0.000 description 1
- 101710089292 Sorcin Proteins 0.000 description 1
- 101710183296 Surface layer protein Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- GAYLGYUVTDMLKC-UWJYBYFXSA-N Tyr-Asp-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 GAYLGYUVTDMLKC-UWJYBYFXSA-N 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- SXEHKFHPFVVDIR-UHFFFAOYSA-N [4-(4-hydrazinylphenyl)phenyl]hydrazine Chemical compound C1=CC(NN)=CC=C1C1=CC=C(NN)C=C1 SXEHKFHPFVVDIR-UHFFFAOYSA-N 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 230000002788 anti-peptide Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 210000003495 flagella Anatomy 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 108010091748 peptide A Proteins 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 238000011533 pre-incubation Methods 0.000 description 1
- 235000019260 propionic acid Nutrition 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000000126 substance Chemical class 0.000 description 1
- 150000003464 sulfur compounds Chemical class 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000012138 yeast extract Substances 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
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
Claims (7)
1. Peptid, kännetecknad därav, att den är ett fragment av ett protein av en Pectinatus-bakteries 5 ytskikt och har Ala Ala Asn Pro Phe Ser Asp Vai Pro Ala Asp Ser Ser Ala Tyr (sekv. nr 3) eller ett derivat därav med sanuna antigena egenskaper, eller Ala Leu Vai Vai Lys Asn Asn Met Ser Ala Leu Asn Thr Leu Asn (sekv. nr 4) eller ett derivat därav med samma antigena egenskaper, som 10 antigen determinant.
2. Peptid enligt patentkrav 1, kännetecknad därav, att den är Ala Ala Asn Pro Phe Ser Asp Vai Pro Ala Asp Ser Ser Ala Tyr (sekv. nr 3) eller ett derivat därav med samma antigena egenskaper.
3. Peptid enligt patentkrav 1, känneteck nad därav, att den är Ala Leu Vai Vai Lys Asn Asn Met Ser Ala Leu Asn Thr Leu Asn (sekv. nr 4) eller ett derivat därav med samma antigena egenskaper.
4. Antikropp, kännetecknad därav, att 20 den är riktad mot en peptid enligt nägot av patentkraven 1 - 3.
5. Antikropp enligt patentkrav 4, kännetecknad därav, att den producerats genom att konju-gera en peptid enligt nägot av patentkraven 1-3 med en ·' 25 bärarmolekyl och sedan använda ifrägavarande konjugat tili immunisering för produktion av antikroppar.
6. Förfarande för pävisning av Pectinatus-bakte-rier, kännetecknat därav, att ett prov, som misstänks innehälla Pectinatus-bakterier, bringas att rea- 30 gera med en antikropp enligt patentkrav 5.
7. Användning av en peptid enligt nägot av patent-kraven 1-3 för framställning av antikroppar. t
Priority Applications (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FI924835A FI94051C (sv) | 1992-10-23 | 1992-10-23 | Proteinfragment av Pectinatus-bakterier |
| EP93922966A EP0666870A1 (en) | 1992-10-23 | 1993-10-21 | PROTEIN FRAGMENTS OF THE $i(PECTINATUS) BACTERIUM |
| JP6510741A JPH08502506A (ja) | 1992-10-23 | 1993-10-21 | ペクチナタス（Ｐｅｃｔｉｎａｔｕｓ）細菌のタンパク断片 |
| PCT/FI1993/000431 WO1994010204A1 (en) | 1992-10-23 | 1993-10-21 | Protein fragments of the pectinatus bacterium |
| AU51785/93A AU5178593A (en) | 1992-10-23 | 1993-10-21 | Protein fragments of the (pectinatus) bacterium |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FI924835A FI94051C (sv) | 1992-10-23 | 1992-10-23 | Proteinfragment av Pectinatus-bakterier |
| FI924835 | 1992-10-23 |
Publications (4)
| Publication Number | Publication Date |
|---|---|
| FI924835A0 FI924835A0 (sv) | 1992-10-23 |
| FI924835A FI924835A (sv) | 1994-04-24 |
| FI94051B FI94051B (sv) | 1995-03-31 |
| FI94051C true FI94051C (sv) | 1995-07-10 |
Family
ID=8536105
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| FI924835A FI94051C (sv) | 1992-10-23 | 1992-10-23 | Proteinfragment av Pectinatus-bakterier |
Country Status (5)
| Country | Link |
|---|---|
| EP (1) | EP0666870A1 (sv) |
| JP (1) | JPH08502506A (sv) |
| AU (1) | AU5178593A (sv) |
| FI (1) | FI94051C (sv) |
| WO (1) | WO1994010204A1 (sv) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE69631413T2 (de) * | 1995-11-28 | 2004-07-08 | Asahi Breweries Ltd. | Nachweis einer bakterie der pectinatus gattung |
-
1992
- 1992-10-23 FI FI924835A patent/FI94051C/sv active IP Right Grant
-
1993
- 1993-10-21 JP JP6510741A patent/JPH08502506A/ja active Pending
- 1993-10-21 AU AU51785/93A patent/AU5178593A/en not_active Abandoned
- 1993-10-21 WO PCT/FI1993/000431 patent/WO1994010204A1/en not_active Application Discontinuation
- 1993-10-21 EP EP93922966A patent/EP0666870A1/en not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| EP0666870A1 (en) | 1995-08-16 |
| FI94051B (sv) | 1995-03-31 |
| FI924835A0 (sv) | 1992-10-23 |
| WO1994010204A1 (en) | 1994-05-11 |
| AU5178593A (en) | 1994-05-24 |
| JPH08502506A (ja) | 1996-03-19 |
| FI924835A (sv) | 1994-04-24 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Fairweather et al. | Immunization of mice against tetanus with fragments of tetanus toxin synthesized in Escherichia coli | |
| EP0558631B1 (en) | Recombinant avirulent salmonella antifertility vaccines | |
| Von Specht et al. | Protection of immunocompromised mice against lethal infection with Pseudomonas aeruginosa by active or passive immunization with recombinant P. aeruginosa outer membrane protein F and outer membrane protein I fusion proteins | |
| JP2003189879A (ja) | 髄膜炎菌（ＮｅｉｓｓｅｒｉａＭｅｎｉｎｇｉｔｉｄｉｓ）のプロテイナーゼＫ抵抗性表面蛋白質 | |
| JPH06277066A (ja) | 髄膜炎菌“Ｎｅｉｓｓｅｒｉａ ｍａｎｉｎｇｉｔｉｄｉｓ”のトランスフェリン受容体のサブユニットをコードするＤＮＡ断片と、その製造方法 | |
| JPH11510373A (ja) | インフルエンザ菌由来のｏｍｐ２６抗原 | |
| CN1304442A (zh) | 用重组耶尔森氏菌将蛋白质送递到真核生物细胞中 | |
| Pellett et al. | Characterization of monoclonal antibodies against the Escherichia coli hemolysin | |
| JPH08509873A (ja) | ヘリコバクター感染に対する免疫組成物、該組成物に用いられるポリペプチドおよび該ポリペプチドをコードする核酸配列 | |
| Cannon | Conserved lipoproteins of pathogenic Neisseria species bearing the H. 8 epitope: lipid-modified azurin and H. 8 outer membrane protein | |
| Hoehn et al. | The major anaerobically induced outer membrane protein of Neisseria gonorrhoeae, Pan 1, is a lipoprotein | |
| 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 | |
| FI102189B (sv) | Förfarande för att producera och isolera PIA-protein av gonorré-bakter ie | |
| Singh et al. | Antigenic determinants of the OmpC porin from Salmonella typhimurium | |
| JP3236610B2 (ja) | 豚胸膜肺炎用ワクチン | |
| Cachia et al. | The use of synthetic peptides in the design of a consensus sequence vaccine for Pseudomonas aeruginosa | |
| FI94051C (sv) | Proteinfragment av Pectinatus-bakterier | |
| Pugsley et al. | Comparison of colicins B-K260 and D-CA23: purification and characterization of the colicins and examination of colicin immunity in the producing strains | |
| Aitken et al. | Amino and carboxy terminal sequences of the DNA-binding protein HU from the Cyanobacterium Synechocystis PCC 6701 (ATCC 27170) | |
| Woods et al. | Characterization of the neisserial lipid‐modified azurin bearing the H. 8 epitope | |
| Aivaliotis et al. | Membrane proteome analysis of the green‐sulfur bacterium Chlorobium tepidum | |
| Michel et al. | Isolation of a photosystem II associated 36 kDa polypeptide and an iron-stress 34 kDa polypeptide from thylakoid membranes of the cyanobacterium Synechococcus PCC 6301 grown under mild iron deficiency | |
| CA2148479A1 (en) | Fibronectin binding protein as well as its preparation | |
| Kamiunten et al. | Subcellular localization of the protein encoded by virulence gene psvA of Pseudomonas syringae pv. eriobotryae | |
| Linhartová | Function of the Type IV pili proteins in the cyanobacterium Synechocystis sp. PCC 6803 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FG | Patent granted |
Owner name: HAKALEHTO, ELIAS |
|
| BB | Publication of examined application |