NO871664L - Fremgangsmaate for fremstilling av dopa-holdige bioadhesivproteiner fra tyrosinholdige proteiner. - Google Patents
Fremgangsmaate for fremstilling av dopa-holdige bioadhesivproteiner fra tyrosinholdige proteiner.Info
- Publication number
- NO871664L NO871664L NO871664A NO871664A NO871664L NO 871664 L NO871664 L NO 871664L NO 871664 A NO871664 A NO 871664A NO 871664 A NO871664 A NO 871664A NO 871664 L NO871664 L NO 871664L
- Authority
- NO
- Norway
- Prior art keywords
- protein
- enzyme
- proteins
- tyrosine
- approx
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims description 64
- 102000004169 proteins and genes Human genes 0.000 title claims description 63
- 239000000227 bioadhesive Substances 0.000 title claims description 25
- 238000000034 method Methods 0.000 title claims description 23
- 238000002360 preparation method Methods 0.000 title description 2
- 238000006243 chemical reaction Methods 0.000 claims description 41
- WTDRDQBEARUVNC-LURJTMIESA-N L-DOPA Chemical group OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-LURJTMIESA-N 0.000 claims description 32
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 claims description 30
- 102000004190 Enzymes Human genes 0.000 claims description 26
- 108090000790 Enzymes Proteins 0.000 claims description 26
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 25
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 25
- 102000003425 Tyrosinase Human genes 0.000 claims description 20
- 108060008724 Tyrosinase Proteins 0.000 claims description 20
- 229960005070 ascorbic acid Drugs 0.000 claims description 15
- 239000000203 mixture Substances 0.000 claims description 7
- 238000011533 pre-incubation Methods 0.000 claims description 7
- 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 claims description 6
- 238000004519 manufacturing process Methods 0.000 claims description 5
- 235000010323 ascorbic acid Nutrition 0.000 claims description 3
- 239000011668 ascorbic acid Substances 0.000 claims description 3
- 239000007790 solid phase Substances 0.000 claims description 3
- 235000001674 Agaricus brunnescens Nutrition 0.000 claims description 2
- 102000014961 Protein Precursors Human genes 0.000 claims description 2
- 108010078762 Protein Precursors Proteins 0.000 claims description 2
- 238000010647 peptide synthesis reaction Methods 0.000 claims description 2
- 230000008569 process Effects 0.000 claims description 2
- 150000004053 quinones Chemical class 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 51
- 235000002374 tyrosine Nutrition 0.000 description 25
- WTDRDQBEARUVNC-UHFFFAOYSA-N L-Dopa Natural products OC(=O)C(N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-UHFFFAOYSA-N 0.000 description 22
- 108090000765 processed proteins & peptides Proteins 0.000 description 17
- 230000015572 biosynthetic process Effects 0.000 description 14
- 239000002211 L-ascorbic acid Substances 0.000 description 12
- 235000000069 L-ascorbic acid Nutrition 0.000 description 12
- 239000012064 sodium phosphate buffer Substances 0.000 description 11
- AZQWKYJCGOJGHM-UHFFFAOYSA-N 1,4-benzoquinone Chemical compound O=C1C=CC(=O)C=C1 AZQWKYJCGOJGHM-UHFFFAOYSA-N 0.000 description 10
- 230000001070 adhesive effect Effects 0.000 description 10
- 239000000758 substrate Substances 0.000 description 10
- 239000000853 adhesive Substances 0.000 description 9
- 230000027455 binding Effects 0.000 description 9
- 238000009739 binding Methods 0.000 description 9
- 235000001014 amino acid Nutrition 0.000 description 8
- 150000001413 amino acids Chemical class 0.000 description 8
- 239000002243 precursor Substances 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 238000003786 synthesis reaction Methods 0.000 description 8
- 229920000642 polymer Polymers 0.000 description 7
- 102000004196 processed proteins & peptides Human genes 0.000 description 7
- 239000005018 casein Substances 0.000 description 6
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 6
- 235000021240 caseins Nutrition 0.000 description 6
- 239000001257 hydrogen Substances 0.000 description 5
- 229910052739 hydrogen Inorganic materials 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 102000008186 Collagen Human genes 0.000 description 4
- 108010035532 Collagen Proteins 0.000 description 4
- 229920001436 collagen Polymers 0.000 description 4
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 102000030523 Catechol oxidase Human genes 0.000 description 3
- 108010031396 Catechol oxidase Proteins 0.000 description 3
- YCIMNLLNPGFGHC-UHFFFAOYSA-N catechol Chemical group OC1=CC=CC=C1O YCIMNLLNPGFGHC-UHFFFAOYSA-N 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 150000003668 tyrosines Chemical class 0.000 description 3
- 241000233866 Fungi Species 0.000 description 2
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 2
- XUMBMVFBXHLACL-UHFFFAOYSA-N Melanin Chemical compound O=C1C(=O)C(C2=CNC3=C(C(C(=O)C4=C32)=O)C)=C2C4=CNC2=C1C XUMBMVFBXHLACL-UHFFFAOYSA-N 0.000 description 2
- 241000237524 Mytilus Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 229910052782 aluminium Inorganic materials 0.000 description 2
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 2
- 150000001412 amines Chemical class 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000007795 chemical reaction product Substances 0.000 description 2
- 239000003638 chemical reducing agent Substances 0.000 description 2
- 238000004132 cross linking Methods 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 230000002538 fungal effect Effects 0.000 description 2
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical compound [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 235000013930 proline Nutrition 0.000 description 2
- 239000011541 reaction mixture Substances 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- RQPKNXVVIBYOBX-KDBLBPRBSA-N (2s)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid;(2s)-2-(dihydroxyamino)-3-phenylpropanoic acid Chemical group OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1.ON(O)[C@H](C(O)=O)CC1=CC=CC=C1 RQPKNXVVIBYOBX-KDBLBPRBSA-N 0.000 description 1
- 150000005206 1,2-dihydroxybenzenes Chemical class 0.000 description 1
- SXGZJKUKBWWHRA-UHFFFAOYSA-N 2-(N-morpholiniumyl)ethanesulfonate Chemical compound [O-]S(=O)(=O)CC[NH+]1CCOCC1 SXGZJKUKBWWHRA-UHFFFAOYSA-N 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000237536 Mytilus edulis Species 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 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
- 238000002835 absorbance Methods 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000006229 amino acid addition Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 239000004568 cement Substances 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 230000007797 corrosion Effects 0.000 description 1
- 238000005260 corrosion Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N cystine group Chemical group C([C@@H](C(=O)O)N)SSC[C@@H](C(=O)O)N LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000011888 foil Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000001879 gelation Methods 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000008595 infiltration Effects 0.000 description 1
- 238000001764 infiltration Methods 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 210000002752 melanocyte Anatomy 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 235000020638 mussel Nutrition 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 238000006396 nitration reaction Methods 0.000 description 1
- 229920000620 organic polymer Polymers 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000012704 polymeric precursor Substances 0.000 description 1
- 150000003148 prolines Chemical class 0.000 description 1
- 230000001681 protective effect Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 125000004151 quinonyl group Chemical group 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000007974 sodium acetate buffer Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 125000003508 trans-4-hydroxy-L-proline group Chemical group 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Adhesives Or Adhesive Processes (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US85659486A | 1986-04-25 | 1986-04-25 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| NO871664D0 NO871664D0 (no) | 1987-04-22 |
| NO871664L true NO871664L (no) | 1987-10-26 |
Family
ID=25324027
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO871664A NO871664L (no) | 1986-04-25 | 1987-04-22 | Fremgangsmaate for fremstilling av dopa-holdige bioadhesivproteiner fra tyrosinholdige proteiner. |
Country Status (6)
| Country | Link |
|---|---|
| EP (1) | EP0242656A3 (da) |
| JP (1) | JPS6328399A (da) |
| AU (1) | AU597353B2 (da) |
| DK (1) | DK163987A (da) |
| FI (1) | FI871726A (da) |
| NO (1) | NO871664L (da) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0332660A4 (en) * | 1986-11-24 | 1990-12-05 | Genex Corporation | Bioadhesives |
| AU1572588A (en) * | 1987-03-12 | 1988-10-10 | Genex Corp. | Production of bioadhesive precursor protein analogs by genetically-engineered organisms |
| US5264569A (en) * | 1990-06-12 | 1993-11-23 | E. I. Du Pont De Nemours And Company | Purified fungal spore tip mucilage |
| WO1991019770A1 (en) * | 1990-06-12 | 1991-12-26 | E.I. Du Pont De Nemours And Company | Fungal adhesive and process of purification |
| US5197973A (en) * | 1990-12-14 | 1993-03-30 | Creative Biomolecules, Inc. | Synthetic bioadhesive |
| DE102004031258A1 (de) * | 2004-06-29 | 2006-02-09 | Jennissen, Herbert P., Prof. Dr. | Proteinhybride mit polyhydroxyaromatischen Aminosäure-Epitopen |
| DE102008057684A1 (de) | 2008-11-17 | 2010-05-20 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Dialkoxy- oder Dihydroxyphenylreste enthaltende Silane, daraus hergestellte Klebstoffe sowie Verfahren zur Herstellung der Silane und der Klebstoffe |
| CN102212568A (zh) * | 2011-03-22 | 2011-10-12 | 深圳大学 | 用酶催化合成药物l-多巴的方法 |
| US20140271500A1 (en) * | 2013-03-14 | 2014-09-18 | Safewhite Llc | Methods and materials for providing teeth with a white appearance |
| US20160115196A1 (en) | 2013-05-28 | 2016-04-28 | Ramot At Tel-Aviv University Ltd. | Self-assembled micro-and nanostructures |
| JP7362096B2 (ja) * | 2018-12-06 | 2023-10-17 | 国立研究開発法人理化学研究所 | 修飾シルクフィブロインタンパク質、及びその利用 |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2447275A1 (fr) * | 1979-01-25 | 1980-08-22 | Charbonnages Ste Chimique | Materiaux stratifies a base de resine phenolique et procede pour leur preparation |
| ZA839115B (en) * | 1982-12-14 | 1984-07-25 | Cpc International Inc | Continuous enzymatic process for producing maltose from starch and starch hydrolysates |
| US4585585A (en) * | 1984-03-07 | 1986-04-29 | University Of Connecticut Research & Development Corporation | Decapeptides produced from bioadhesive polyphenolic proteins |
| EP0332660A4 (en) * | 1986-11-24 | 1990-12-05 | Genex Corporation | Bioadhesives |
-
1987
- 1987-03-31 DK DK163987A patent/DK163987A/da not_active IP Right Cessation
- 1987-04-02 EP EP87104853A patent/EP0242656A3/en not_active Withdrawn
- 1987-04-21 FI FI871726A patent/FI871726A/fi not_active IP Right Cessation
- 1987-04-22 NO NO871664A patent/NO871664L/no unknown
- 1987-04-23 AU AU71887/87A patent/AU597353B2/en not_active Expired - Fee Related
- 1987-04-24 JP JP10020887A patent/JPS6328399A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| AU597353B2 (en) | 1990-05-31 |
| DK163987D0 (da) | 1987-03-31 |
| AU7188787A (en) | 1987-10-29 |
| FI871726A (fi) | 1987-10-26 |
| JPS6328399A (ja) | 1988-02-06 |
| DK163987A (da) | 1987-10-26 |
| FI871726A0 (fi) | 1987-04-21 |
| NO871664D0 (no) | 1987-04-22 |
| EP0242656A2 (en) | 1987-10-28 |
| EP0242656A3 (en) | 1989-04-19 |
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