JP4378052B2 - タイセイヨウサケ由来の孵化液の抽出方法および使用 - Google Patents
タイセイヨウサケ由来の孵化液の抽出方法および使用 Download PDFInfo
- Publication number
- JP4378052B2 JP4378052B2 JP2000524409A JP2000524409A JP4378052B2 JP 4378052 B2 JP4378052 B2 JP 4378052B2 JP 2000524409 A JP2000524409 A JP 2000524409A JP 2000524409 A JP2000524409 A JP 2000524409A JP 4378052 B2 JP4378052 B2 JP 4378052B2
- Authority
- JP
- Japan
- Prior art keywords
- salmon
- solution
- preparation
- serine endoprotease
- zonase
- 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.)
- Expired - Lifetime
Links
- 241000277263 Salmo Species 0.000 title abstract description 7
- 238000000605 extraction Methods 0.000 title 1
- 241000972773 Aulopiformes Species 0.000 claims abstract description 25
- 235000019515 salmon Nutrition 0.000 claims abstract description 25
- 238000000034 method Methods 0.000 claims abstract description 24
- 238000002360 preparation method Methods 0.000 claims abstract description 22
- 101710118538 Protease Proteins 0.000 claims abstract description 18
- 235000013601 eggs Nutrition 0.000 claims abstract description 13
- 230000012447 hatching Effects 0.000 claims abstract description 12
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims abstract description 9
- 239000004202 carbamide Substances 0.000 claims abstract description 9
- 238000001042 affinity chromatography Methods 0.000 claims abstract description 8
- 238000002523 gelfiltration Methods 0.000 claims abstract description 8
- 230000000694 effects Effects 0.000 claims abstract description 5
- 238000001914 filtration Methods 0.000 claims abstract description 5
- 230000017854 proteolysis Effects 0.000 claims abstract description 4
- 230000001360 synchronised effect Effects 0.000 claims abstract description 4
- 102000004190 Enzymes Human genes 0.000 claims description 17
- 108090000790 Enzymes Proteins 0.000 claims description 17
- 108090000623 proteins and genes Proteins 0.000 claims description 14
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 13
- 102000004169 proteins and genes Human genes 0.000 claims description 13
- 102000002322 Egg Proteins Human genes 0.000 claims description 9
- 210000003278 egg shell Anatomy 0.000 claims description 9
- 108010000912 Egg Proteins Proteins 0.000 claims description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 7
- PXXJHWLDUBFPOL-UHFFFAOYSA-N benzamidine Chemical compound NC(=N)C1=CC=CC=C1 PXXJHWLDUBFPOL-UHFFFAOYSA-N 0.000 claims description 6
- 239000003960 organic solvent Substances 0.000 claims description 6
- 150000003839 salts Chemical class 0.000 claims description 6
- 239000012634 fragment Substances 0.000 claims description 5
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 claims description 5
- 239000003112 inhibitor Substances 0.000 claims description 4
- 239000011159 matrix material Substances 0.000 claims description 4
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 claims description 3
- 239000012506 Sephacryl® Substances 0.000 claims description 3
- 238000004458 analytical method Methods 0.000 claims description 3
- 238000004587 chromatography analysis Methods 0.000 claims description 3
- 238000010828 elution Methods 0.000 claims description 3
- 238000000464 low-speed centrifugation Methods 0.000 claims description 3
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims description 3
- 239000004475 Arginine Substances 0.000 claims description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 2
- 239000012153 distilled water Substances 0.000 claims description 2
- 238000001704 evaporation Methods 0.000 claims description 2
- 230000008020 evaporation Effects 0.000 claims description 2
- 230000002401 inhibitory effect Effects 0.000 claims description 2
- BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 claims description 2
- 239000000243 solution Substances 0.000 claims 9
- 238000004255 ion exchange chromatography Methods 0.000 claims 4
- 125000000532 dioxanyl group Chemical group 0.000 claims 2
- 238000011534 incubation Methods 0.000 claims 2
- 230000001939 inductive effect Effects 0.000 claims 2
- 239000012266 salt solution Substances 0.000 claims 2
- 239000007787 solid Substances 0.000 claims 2
- 239000006228 supernatant Substances 0.000 claims 2
- 239000012504 chromatography matrix Substances 0.000 claims 1
- 239000011356 non-aqueous organic solvent Substances 0.000 claims 1
- 238000001243 protein synthesis Methods 0.000 claims 1
- 230000014616 translation Effects 0.000 claims 1
- 238000006555 catalytic reaction Methods 0.000 abstract description 5
- 230000002255 enzymatic effect Effects 0.000 abstract description 4
- 239000000706 filtrate Substances 0.000 abstract description 3
- 239000012530 fluid Substances 0.000 abstract description 2
- 238000005119 centrifugation Methods 0.000 abstract 1
- 235000013351 cheese Nutrition 0.000 abstract 1
- 239000004744 fabric Substances 0.000 abstract 1
- 238000001155 isoelectric focusing Methods 0.000 abstract 1
- 229940088598 enzyme Drugs 0.000 description 16
- 238000000746 purification Methods 0.000 description 14
- 239000000758 substrate Substances 0.000 description 9
- 102000012479 Serine Proteases Human genes 0.000 description 8
- 108010022999 Serine Proteases Proteins 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
- 108090000765 processed proteins & peptides Proteins 0.000 description 6
- 102000004142 Trypsin Human genes 0.000 description 5
- 108090000631 Trypsin Proteins 0.000 description 5
- 230000003197 catalytic effect Effects 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000012588 trypsin Substances 0.000 description 5
- 150000001413 amino acids Chemical group 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
- 241000251468 Actinopterygii Species 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 210000002257 embryonic structure Anatomy 0.000 description 3
- 235000019688 fish Nutrition 0.000 description 3
- 102000036437 hatching enzymes Human genes 0.000 description 3
- 108091007166 hatching enzymes Proteins 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 239000007858 starting material Substances 0.000 description 3
- 102000005741 Metalloproteases Human genes 0.000 description 2
- 108010006035 Metalloproteases Proteins 0.000 description 2
- 238000011210 chromatographic step Methods 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 210000001161 mammalian embryo Anatomy 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- RNAMYOYQYRYFQY-UHFFFAOYSA-N 2-(4,4-difluoropiperidin-1-yl)-6-methoxy-n-(1-propan-2-ylpiperidin-4-yl)-7-(3-pyrrolidin-1-ylpropoxy)quinazolin-4-amine Chemical compound N1=C(N2CCC(F)(F)CC2)N=C2C=C(OCCCN3CCCC3)C(OC)=CC2=C1NC1CCN(C(C)C)CC1 RNAMYOYQYRYFQY-UHFFFAOYSA-N 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 101710089350 Eggshell protein Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- -1 NaCl salt Chemical class 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-N acetic acid Substances CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 238000012443 analytical study Methods 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 238000009360 aquaculture Methods 0.000 description 1
- 244000144974 aquaculture Species 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000013058 crude material Substances 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000006392 deoxygenation reaction Methods 0.000 description 1
- 229940079919 digestives enzyme preparation Drugs 0.000 description 1
- 230000003241 endoproteolytic effect Effects 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 239000013542 high molecular weight contaminant Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 238000000734 protein sequencing Methods 0.000 description 1
- 239000003001 serine protease inhibitor Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- PIEPQKCYPFFYMG-UHFFFAOYSA-N tris acetate Chemical compound CC(O)=O.OCC(N)(CO)CO PIEPQKCYPFFYMG-UHFFFAOYSA-N 0.000 description 1
- 239000002351 wastewater Substances 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6402—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
Landscapes
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Meat, Egg Or Seafood Products (AREA)
- Peptides Or Proteins (AREA)
- Saccharide Compounds (AREA)
- Extraction Or Liquid Replacement (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| NO19975826A NO314594B1 (no) | 1997-12-11 | 1997-12-11 | Ikke-selvdegraderende endoprotease, fremgangsmåte for fremstilling samt anvendelser av denne |
| NO19975826 | 1997-12-11 | ||
| PCT/NO1998/000378 WO1999029836A1 (en) | 1997-12-11 | 1998-12-11 | Procedure for extraction and use of hatching fluid from atlantic salmon |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2001526026A JP2001526026A (ja) | 2001-12-18 |
| JP2001526026A5 JP2001526026A5 (enExample) | 2005-08-04 |
| JP4378052B2 true JP4378052B2 (ja) | 2009-12-02 |
Family
ID=19901439
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000524409A Expired - Lifetime JP4378052B2 (ja) | 1997-12-11 | 1998-12-11 | タイセイヨウサケ由来の孵化液の抽出方法および使用 |
Country Status (14)
| Country | Link |
|---|---|
| US (1) | US6346245B1 (enExample) |
| EP (1) | EP1036166B1 (enExample) |
| JP (1) | JP4378052B2 (enExample) |
| AT (1) | ATE328072T1 (enExample) |
| AU (1) | AU761292B2 (enExample) |
| CA (1) | CA2314608C (enExample) |
| CY (1) | CY1105206T1 (enExample) |
| DE (1) | DE69834742T2 (enExample) |
| DK (1) | DK1036166T3 (enExample) |
| ES (1) | ES2264223T3 (enExample) |
| NO (1) | NO314594B1 (enExample) |
| NZ (1) | NZ504865A (enExample) |
| PT (1) | PT1036166E (enExample) |
| WO (1) | WO1999029836A1 (enExample) |
Families Citing this family (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6960451B2 (en) | 2002-02-06 | 2005-11-01 | Green Earth Industries | Proteolytic fermenter |
| US7756573B2 (en) | 2006-09-05 | 2010-07-13 | Cardiac Pacemakers, Inc. | Implantable medical device diagnostic data acquisition and storage |
| GB0819883D0 (en) * | 2008-10-29 | 2008-12-03 | Azyme Res As | Product and uses |
| US8970707B2 (en) | 2008-12-17 | 2015-03-03 | Sony Computer Entertainment Inc. | Compensating for blooming of a shape in an image |
| CN102471766A (zh) * | 2009-07-17 | 2012-05-23 | 科洛普拉斯特公司 | 带有酶的粘性贴片 |
| GB0921001D0 (en) | 2009-11-30 | 2010-01-13 | Aqua Bio Technology Asa | Products and uses |
| GB201007202D0 (en) | 2010-04-29 | 2010-06-16 | Walther Bernt T | Product and uses |
| NO335697B1 (no) | 2010-05-25 | 2015-01-26 | Alvestad As | Anvendelse av anordning for separasjon av proteiner fra klekkevæske |
| GB201110777D0 (en) | 2011-06-24 | 2011-08-10 | Aqua Bio Technology Asa | Methods and uses |
| GB201110783D0 (en) | 2011-06-24 | 2011-08-10 | Aqua Bio Technology Asa | Methods and uses |
| AP2014007818A0 (en) | 2012-01-23 | 2014-07-31 | Restorsea Llc | Cosmetic |
| CN105025906B (zh) * | 2012-12-21 | 2020-08-25 | 阿克生物科技公司 | 来自鱼孵化液的化妆品组合物 |
| GB201223330D0 (en) * | 2012-12-21 | 2013-02-06 | Aqua Bio Technology Asa | Products, methods and uses |
| CN105813627A (zh) | 2013-12-13 | 2016-07-27 | 雷斯托尔西有限公司 | 脱落毛发保留促进的制剂 |
| KR20170003691A (ko) | 2014-05-16 | 2017-01-09 | 레스토시, 엘엘씨 | 2상 화장료 |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5077393A (en) * | 1987-05-25 | 1991-12-31 | Research Development Corporation Of Japan | Method for producing vitronectin |
-
1997
- 1997-12-11 NO NO19975826A patent/NO314594B1/no not_active IP Right Cessation
-
1998
- 1998-12-11 DE DE69834742T patent/DE69834742T2/de not_active Expired - Lifetime
- 1998-12-11 WO PCT/NO1998/000378 patent/WO1999029836A1/en not_active Ceased
- 1998-12-11 EP EP98962724A patent/EP1036166B1/en not_active Expired - Lifetime
- 1998-12-11 ES ES98962724T patent/ES2264223T3/es not_active Expired - Lifetime
- 1998-12-11 JP JP2000524409A patent/JP4378052B2/ja not_active Expired - Lifetime
- 1998-12-11 US US09/581,026 patent/US6346245B1/en not_active Expired - Lifetime
- 1998-12-11 NZ NZ504865A patent/NZ504865A/xx not_active IP Right Cessation
- 1998-12-11 AT AT98962724T patent/ATE328072T1/de active
- 1998-12-11 CA CA2314608A patent/CA2314608C/en not_active Expired - Lifetime
- 1998-12-11 AU AU17894/99A patent/AU761292B2/en not_active Expired
- 1998-12-11 DK DK98962724T patent/DK1036166T3/da active
- 1998-12-11 PT PT98962724T patent/PT1036166E/pt unknown
-
2006
- 2006-08-30 CY CY20061101219T patent/CY1105206T1/el unknown
Also Published As
| Publication number | Publication date |
|---|---|
| NO975826L (no) | 1999-06-14 |
| CA2314608C (en) | 2013-01-22 |
| DE69834742T2 (de) | 2007-05-31 |
| US6346245B1 (en) | 2002-02-12 |
| AU761292B2 (en) | 2003-05-29 |
| CY1105206T1 (el) | 2010-03-03 |
| AU1789499A (en) | 1999-06-28 |
| DE69834742D1 (de) | 2006-07-06 |
| EP1036166A1 (en) | 2000-09-20 |
| NO975826D0 (no) | 1997-12-11 |
| ES2264223T3 (es) | 2006-12-16 |
| NO314594B1 (no) | 2003-04-14 |
| EP1036166B1 (en) | 2006-05-31 |
| PT1036166E (pt) | 2006-09-29 |
| DK1036166T3 (da) | 2006-09-25 |
| JP2001526026A (ja) | 2001-12-18 |
| HK1030968A1 (en) | 2001-05-25 |
| ATE328072T1 (de) | 2006-06-15 |
| WO1999029836A1 (en) | 1999-06-17 |
| NZ504865A (en) | 2002-12-20 |
| CA2314608A1 (en) | 1999-06-17 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4378052B2 (ja) | タイセイヨウサケ由来の孵化液の抽出方法および使用 | |
| Cao et al. | Identification of a myofibril-bound serine proteinase (MBSP) in the skeletal muscle of lizard fish Saurida wanieso which specifically cleaves the arginine site | |
| US5270176A (en) | Method for the selective cleavage of fusion proteins with lysostaphin | |
| Neurath et al. | Purification and properties of a trypsin-like enzyme from the starfish Evasterias trochelii | |
| JPH02504465A (ja) | オキアミ組織からの活性酵素の単離の改良 | |
| US6592866B2 (en) | Non-selfdegrading endoprotease | |
| US12325868B2 (en) | Purified fish proteases with high specific activities and its process of production | |
| De Haen et al. | Isolation and amino-terminal sequence analysis of a new pancreatic trypsinogen of the African lungfish Protopterus aethiopicus | |
| JPS6023085B2 (ja) | アンジオテンシン転換酵素阻害剤 | |
| Song et al. | Chromatographic purification of the plasmin‐like enzyme from clamworm (Perinereis aibuhitensis Grub) and its fibrinolytic activity by metal ions | |
| HK1030968B (en) | Procedure for extraction and use of hatching fluid from atlantic salmon | |
| Dubé | Prostatic kallikreins: biochemistry and physiology | |
| Słowińska et al. | Identification of the second form of acrosin in turkey spermatozoa | |
| Tamori et al. | Purification and characterization of a novel isoform of myosinase from spear squid liver | |
| Gudzenko et al. | Purification and physico-chemical properties of Bacillus atrophaeus protease with elastolytic and fibrinogenolytic activity | |
| JP4355287B2 (ja) | ホッコクアカエビ由来の新規なカテプシンｌ様システインプロテアーゼ | |
| Nakano et al. | Studies on a protamine (galline) from fowl sperm. 4. Degradation of galline by trypsin‐like protease of fowl sperm heads | |
| ABDEL-FATTAH et al. | Purification and proteolytic action of milk-clotting enzyme produced by Penicillium citrinum | |
| RU1807080C (ru) | Способ выделени амилазы из препарата амилоризин | |
| Tshidino | PURIFICATION AND PARTIAL CHARACTERIZATION OF A MYOFIBRIL-BOUND SERINE PROTEASE AND ITS ENDOGENOUS INHIBITOR FROM SKELETAL MUSCLE OF THE OSTRICH | |
| US3313711A (en) | Preparation of aminopeptidase | |
| Shukri | Activation of prorennin | |
| Jiang | Cloning and characterization of midgut-specific gene/gene products in the mosquito Aedes aegypti | |
| JP2006067804A (ja) | ウニ内臓由来プロテアーゼ | |
| JPH05170921A (ja) | エラスチン水溶液の製造方法 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20070626 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20070914 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20070925 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20071017 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20071024 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20071226 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20080909 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20081208 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20081215 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20090109 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20090224 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20090519 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20090701 |
|
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
| R155 | Notification before disposition of declining of application |
Free format text: JAPANESE INTERMEDIATE CODE: R155 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20090914 |
|
| R150 | Certificate of patent or registration of utility model |
Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20120918 Year of fee payment: 3 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130918 Year of fee payment: 4 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| EXPY | Cancellation because of completion of term |