FI119024B - Kimeriska avidinmutanter - Google Patents
Kimeriska avidinmutanter Download PDFInfo
- Publication number
- FI119024B FI119024B FI20041705A FI20041705A FI119024B FI 119024 B FI119024 B FI 119024B FI 20041705 A FI20041705 A FI 20041705A FI 20041705 A FI20041705 A FI 20041705A FI 119024 B FI119024 B FI 119024B
- Authority
- FI
- Finland
- Prior art keywords
- avidin
- avr4
- protein
- proteins
- biotin
- Prior art date
Links
- 108090001008 Avidin Proteins 0.000 title claims abstract description 115
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 74
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 70
- 101150072119 Avr4 gene Proteins 0.000 claims description 104
- 238000000034 method Methods 0.000 claims description 7
- 125000000539 amino acid group Chemical group 0.000 claims description 6
- 239000013598 vector Substances 0.000 claims description 3
- 108091033319 polynucleotide Proteins 0.000 claims 3
- 102000040430 polynucleotide Human genes 0.000 claims 3
- 239000002157 polynucleotide Substances 0.000 claims 3
- 125000003275 alpha amino acid group Chemical group 0.000 claims 2
- 239000001963 growth medium Substances 0.000 claims 2
- 108091028043 Nucleic acid sequence Proteins 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 claims 1
- 230000017854 proteolysis Effects 0.000 abstract description 4
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 86
- 235000018102 proteins Nutrition 0.000 description 65
- 229960002685 biotin Drugs 0.000 description 42
- 235000020958 biotin Nutrition 0.000 description 42
- 239000011616 biotin Substances 0.000 description 42
- 230000027455 binding Effects 0.000 description 26
- 238000010494 dissociation reaction Methods 0.000 description 23
- 230000005593 dissociations Effects 0.000 description 23
- 102220623518 Immunoglobulin heavy variable 4-61_I117Y_mutation Human genes 0.000 description 20
- 238000003556 assay Methods 0.000 description 11
- 108010067770 Endopeptidase K Proteins 0.000 description 10
- 230000035772 mutation Effects 0.000 description 10
- 150000001413 amino acids Chemical class 0.000 description 8
- 235000001014 amino acid Nutrition 0.000 description 7
- 229940024606 amino acid Drugs 0.000 description 7
- 238000000113 differential scanning calorimetry Methods 0.000 description 7
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 6
- WWVANQJRLPIHNS-BKPPORCPSA-N 2-iminobiotin Chemical compound N1C(=N)N[C@H]2[C@H](CCCCC(=O)O)SC[C@H]21 WWVANQJRLPIHNS-BKPPORCPSA-N 0.000 description 5
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- 108091005804 Peptidases Proteins 0.000 description 5
- 239000004365 Protease Substances 0.000 description 5
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 5
- 230000000875 corresponding effect Effects 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 239000012467 final product Substances 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 108020001507 fusion proteins Proteins 0.000 description 5
- 238000002523 gelfiltration Methods 0.000 description 5
- 230000013595 glycosylation Effects 0.000 description 5
- 238000006206 glycosylation reaction Methods 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 230000003287 optical effect Effects 0.000 description 5
- 230000002688 persistence Effects 0.000 description 5
- 235000019419 proteases Nutrition 0.000 description 5
- 238000012546 transfer Methods 0.000 description 5
- 241000287828 Gallus gallus Species 0.000 description 4
- 241000238631 Hexapoda Species 0.000 description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 4
- 125000003118 aryl group Chemical group 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 4
- 108010090804 Streptavidin Proteins 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- 108700021042 biotin binding protein Proteins 0.000 description 3
- 102000043871 biotin binding protein Human genes 0.000 description 3
- 125000000837 carbohydrate group Chemical group 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 230000007704 transition Effects 0.000 description 3
- 241000271566 Aves Species 0.000 description 2
- 238000001712 DNA sequencing Methods 0.000 description 2
- 241000588724 Escherichia coli Species 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
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 239000000872 buffer Substances 0.000 description 2
- 238000007707 calorimetry Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 230000000052 comparative effect Effects 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 150000002500 ions Chemical class 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 235000014705 isoleucine Nutrition 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 230000002085 persistent effect Effects 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 239000000700 radioactive tracer Substances 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 229910052710 silicon Inorganic materials 0.000 description 2
- 239000010703 silicon Substances 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- DEQPBRIACBATHE-FXQIFTODSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-2-iminopentanoic acid Chemical compound N1C(=O)N[C@@H]2[C@H](CCCC(=N)C(=O)O)SC[C@@H]21 DEQPBRIACBATHE-FXQIFTODSA-N 0.000 description 1
- 101800000263 Acidic protein Proteins 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102000006410 Apoproteins Human genes 0.000 description 1
- 108010083590 Apoproteins Proteins 0.000 description 1
- 108010056594 Avian Proteins Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 101100437155 Gallus gallus AVR2 gene Proteins 0.000 description 1
- 101100437158 Gallus gallus AVR5 gene Proteins 0.000 description 1
- HLRLXVPRJJITSK-IFFSRLJSSA-N Gln-Thr-Val Chemical group [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(O)=O HLRLXVPRJJITSK-IFFSRLJSSA-N 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 102220491927 Golgin subfamily A member 6-like protein 2_N54H_mutation Human genes 0.000 description 1
- RNKSNIBMTUYWSH-YFKPBYRVSA-N L-prolylglycine Chemical compound [O-]C(=O)CNC(=O)[C@@H]1CCC[NH2+]1 RNKSNIBMTUYWSH-YFKPBYRVSA-N 0.000 description 1
- 101710093543 Probable non-specific lipid-transfer protein Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 102220465574 Putative uncharacterized protein OBSCN-AS1_A39D_mutation Human genes 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 238000013320 baculovirus expression vector system Methods 0.000 description 1
- 238000013321 baculovirus-insect cell expression system Methods 0.000 description 1
- 238000005452 bending Methods 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 1
- 229960004316 cisplatin Drugs 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 125000004093 cyano group Chemical group *C#N 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 229940068840 d-biotin Drugs 0.000 description 1
- 230000003247 decreasing effect Effects 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
- 238000010586 diagram Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 201000008659 immature cataract Diseases 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000000670 ligand binding assay Methods 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 238000000302 molecular modelling Methods 0.000 description 1
- 238000006384 oligomerization reaction Methods 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 244000045947 parasite Species 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 108010029020 prolylglycine Proteins 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 102200129657 rs35278779 Human genes 0.000 description 1
- 102220114585 rs886039132 Human genes 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000007619 statistical method Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 230000006918 subunit interaction Effects 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 150000003722 vitamin derivatives Chemical class 0.000 description 1
- 238000012982 x-ray structure analysis Methods 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
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/465—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from birds
Claims (7)
1. Chimär avidinmutant, kännetecknad av att aminosyrarester 38-60 av vildtyp avidin ersätts med aminosyrarester 38-58 frän AVR4/5 och att dess aminosyra-sekvens kodas av DNA-sekvensen SEQ ID NO: 15.
2. Chimär avidinmutant, som har aminosyrasekvensen SEQ ID NO: 16.
3. Isolerad polynukleotid, som kodar chimär avidinmutant i enlighet med patentkrav 1 eller 2.
4. Rekombinantvektor, som innefattar en polynukleotid i enlighet med patentkrav 3.
5. Rekombinant värdcell, som innefattar en polynukleotid i enlighet med patent krav 3 eller en rekombinantvektor i enlighet med patentkrav 4.
6. Förfarande för producering av en chimär avidinmutant, kännetecknat av att en rekombinant värdcell i enlighet med patentkrav 5 odlas i odlingsmedium och en chimär avidinmutant samlas in frän odlingsmediet. 15
7. Förfarande för tillverkning av chimär avidinmutant med förbättrad stabilitet, kännetecknat av att aminosyrarester 38-60 av vildtyp avidin (SEQ ID NO: 1) er- ϊsätts med rester 38-58 av protein AVR4/5 (SEQ ID NO: 5 och SEQ ID NO: 6). ··1 2 1 • ·· • 1 ♦ · **♦ »· • · : ·· • 1 ·♦· ···· ·#♦ • · • · ·· • · • ·· • · • ♦ ··· · • · · • 1♦ • · • · 2 • · : ·· • · • 1 · • ·« • #
Priority Applications (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FI20041705A FI119024B (sv) | 2004-12-31 | 2004-12-31 | Kimeriska avidinmutanter |
| AT05112190T ATE481418T1 (de) | 2004-12-31 | 2005-12-15 | Chimäre avidinmutanten |
| DE602005023576T DE602005023576D1 (de) | 2004-12-31 | 2005-12-15 | Chimäre Avidinmutanten |
| EP05112190A EP1676858B1 (en) | 2004-12-31 | 2005-12-15 | Chimeric avidin mutants |
| US11/321,685 US7268216B2 (en) | 2004-12-31 | 2005-12-29 | Chimeric avidin mutants |
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| FI20041705 | 2004-12-31 | ||
| FI20041705A FI119024B (sv) | 2004-12-31 | 2004-12-31 | Kimeriska avidinmutanter |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| FI20041705A0 FI20041705A0 (sv) | 2004-12-31 |
| FI20041705A FI20041705A (sv) | 2006-07-01 |
| FI119024B true FI119024B (sv) | 2008-06-30 |
Family
ID=33548062
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| FI20041705A FI119024B (sv) | 2004-12-31 | 2004-12-31 | Kimeriska avidinmutanter |
Country Status (5)
| Country | Link |
|---|---|
| US (1) | US7268216B2 (sv) |
| EP (1) | EP1676858B1 (sv) |
| AT (1) | ATE481418T1 (sv) |
| DE (1) | DE602005023576D1 (sv) |
| FI (1) | FI119024B (sv) |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FI20021518A0 (sv) | 2002-08-23 | 2002-08-23 | Jyvaeskylaen Yliopisto | Ökning av avidinets värmetålighet |
-
2004
- 2004-12-31 FI FI20041705A patent/FI119024B/sv active IP Right Grant
-
2005
- 2005-12-15 EP EP05112190A patent/EP1676858B1/en active Active
- 2005-12-15 DE DE602005023576T patent/DE602005023576D1/de active Active
- 2005-12-15 AT AT05112190T patent/ATE481418T1/de not_active IP Right Cessation
- 2005-12-29 US US11/321,685 patent/US7268216B2/en active Active
Also Published As
| Publication number | Publication date |
|---|---|
| EP1676858B1 (en) | 2010-09-15 |
| EP1676858A3 (en) | 2008-02-13 |
| FI20041705A (sv) | 2006-07-01 |
| DE602005023576D1 (de) | 2010-10-28 |
| ATE481418T1 (de) | 2010-10-15 |
| EP1676858A2 (en) | 2006-07-05 |
| FI20041705A0 (sv) | 2004-12-31 |
| US20060172387A1 (en) | 2006-08-03 |
| US7268216B2 (en) | 2007-09-11 |
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