JP2018186837A5 - - Google Patents
Download PDFInfo
- Publication number
- JP2018186837A5 JP2018186837A5 JP2018166687A JP2018166687A JP2018186837A5 JP 2018186837 A5 JP2018186837 A5 JP 2018186837A5 JP 2018166687 A JP2018166687 A JP 2018166687A JP 2018166687 A JP2018166687 A JP 2018166687A JP 2018186837 A5 JP2018186837 A5 JP 2018186837A5
- Authority
- JP
- Japan
- Prior art keywords
- amino acid
- seq
- leucine
- histidine
- isoleucine
- 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.)
- Granted
Links
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims 96
- 235000001014 amino acid Nutrition 0.000 claims 78
- 229940024606 amino acid Drugs 0.000 claims 73
- 150000001413 amino acids Chemical class 0.000 claims 72
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims 63
- 235000005772 leucine Nutrition 0.000 claims 63
- 229960003136 leucine Drugs 0.000 claims 63
- 125000003275 alpha amino acid group Chemical group 0.000 claims 61
- 108010078123 amadoriase Proteins 0.000 claims 57
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims 56
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 claims 53
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims 53
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims 53
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims 53
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims 53
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims 53
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims 53
- 235000018417 cysteine Nutrition 0.000 claims 53
- 229960002433 cysteine Drugs 0.000 claims 53
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims 53
- 235000014705 isoleucine Nutrition 0.000 claims 53
- 229960000310 isoleucine Drugs 0.000 claims 53
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims 53
- 235000006109 methionine Nutrition 0.000 claims 53
- 229930182817 methionine Natural products 0.000 claims 53
- 229960004452 methionine Drugs 0.000 claims 53
- 235000013930 proline Nutrition 0.000 claims 53
- 229960002429 proline Drugs 0.000 claims 53
- 229960004799 tryptophan Drugs 0.000 claims 53
- 235000014393 valine Nutrition 0.000 claims 53
- 229960004295 valine Drugs 0.000 claims 53
- 239000004474 valine Substances 0.000 claims 53
- 239000004471 Glycine Substances 0.000 claims 52
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims 52
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims 52
- 229960002449 glycine Drugs 0.000 claims 52
- 235000002374 tyrosine Nutrition 0.000 claims 52
- 229960004441 tyrosine Drugs 0.000 claims 52
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims 52
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims 51
- 235000008729 phenylalanine Nutrition 0.000 claims 51
- 229960005190 phenylalanine Drugs 0.000 claims 51
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims 51
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims 49
- 235000014304 histidine Nutrition 0.000 claims 48
- 229960002885 histidine Drugs 0.000 claims 48
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Chemical group OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims 48
- 239000004472 Lysine Chemical group 0.000 claims 47
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Chemical group NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims 47
- 235000018977 lysine Nutrition 0.000 claims 47
- 229960003646 lysine Drugs 0.000 claims 47
- 239000004475 Arginine Substances 0.000 claims 44
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims 44
- 235000009697 arginine Nutrition 0.000 claims 44
- 229960003121 arginine Drugs 0.000 claims 44
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims 44
- 235000004400 serine Nutrition 0.000 claims 44
- 229960001153 serine Drugs 0.000 claims 44
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims 43
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims 43
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims 43
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical group NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims 43
- 235000009582 asparagine Nutrition 0.000 claims 43
- 229960001230 asparagine Drugs 0.000 claims 43
- 235000004554 glutamine Nutrition 0.000 claims 43
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims 43
- 229960002743 glutamine Drugs 0.000 claims 43
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims 42
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical group OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims 42
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims 42
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims 42
- 239000004473 Threonine Substances 0.000 claims 42
- 235000008521 threonine Nutrition 0.000 claims 42
- 229960002898 threonine Drugs 0.000 claims 42
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims 40
- 235000004279 alanine Nutrition 0.000 claims 34
- 229960003767 alanine Drugs 0.000 claims 34
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical group C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims 33
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims 25
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims 25
- 235000013922 glutamic acid Nutrition 0.000 claims 25
- 229960002989 glutamic acid Drugs 0.000 claims 25
- 239000004220 glutamic acid Substances 0.000 claims 25
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 24
- 235000003704 aspartic acid Nutrition 0.000 claims 24
- 229960005261 aspartic acid Drugs 0.000 claims 24
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims 24
- 230000000694 effects Effects 0.000 claims 15
- -1 α-fructosyl Chemical group 0.000 claims 13
- 230000009257 reactivity Effects 0.000 claims 10
- 238000006467 substitution reaction Methods 0.000 claims 9
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 claims 8
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 claims 7
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 claims 6
- 238000000034 method Methods 0.000 claims 6
- 125000000539 amino acid group Chemical group 0.000 claims 4
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 claims 4
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 claims 4
- 239000002773 nucleotide Substances 0.000 claims 3
- 125000003729 nucleotide group Chemical group 0.000 claims 3
- 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 3
- 241001337994 Cryptococcus <scale insect> Species 0.000 claims 2
- 241000235035 Debaryomyces Species 0.000 claims 2
- 241000228138 Emericella Species 0.000 claims 2
- 241000223609 Microascus Species 0.000 claims 2
- 241000228143 Penicillium Species 0.000 claims 2
- 108091005804 Peptidases Proteins 0.000 claims 2
- 241000235648 Pichia Species 0.000 claims 2
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 claims 2
- 241000868613 Achaetomium sp. Species 0.000 claims 1
- 241000589158 Agrobacterium Species 0.000 claims 1
- 241000171738 Arthrinium Species 0.000 claims 1
- 241000186063 Arthrobacter Species 0.000 claims 1
- 241000228257 Aspergillus sp. Species 0.000 claims 1
- 241000221955 Chaetomium Species 0.000 claims 1
- 241001327444 Coniochaeta Species 0.000 claims 1
- 241001340163 Coniochaetidium Species 0.000 claims 1
- 241000186216 Corynebacterium Species 0.000 claims 1
- 241000223208 Curvularia Species 0.000 claims 1
- 241001149959 Fusarium sp. Species 0.000 claims 1
- 241001149562 Gelasinospora Species 0.000 claims 1
- 241000228456 Leptosphaeria Species 0.000 claims 1
- 241000124176 Neocosmospora Species 0.000 claims 1
- 241000190509 Ophiobolus Species 0.000 claims 1
- 241000228168 Penicillium sp. Species 0.000 claims 1
- 102000035195 Peptidases Human genes 0.000 claims 1
- 241000555275 Phaeosphaeria Species 0.000 claims 1
- 241001136503 Pleospora Species 0.000 claims 1
- 239000004365 Protease Substances 0.000 claims 1
- 241000812330 Pyrenochaeta Species 0.000 claims 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- 241001494489 Thielavia Species 0.000 claims 1
- 241000266300 Ulocladium Species 0.000 claims 1
- BNQVUHQWZGTIBX-IUCAKERBSA-N Val-His Chemical compound CC(C)[C@H]([NH3+])C(=O)N[C@H](C([O-])=O)CC1=CN=CN1 BNQVUHQWZGTIBX-IUCAKERBSA-N 0.000 claims 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 claims 1
- 230000000295 complement effect Effects 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims 1
- 238000005259 measurement Methods 0.000 claims 1
- 230000004048 modification Effects 0.000 claims 1
- 238000012986 modification Methods 0.000 claims 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims 1
- 235000019833 protease Nutrition 0.000 claims 1
- 235000019419 proteases Nutrition 0.000 claims 1
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 claims 1
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2012102771 | 2012-04-27 | ||
| JP2012102771 | 2012-04-27 |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014512732A Division JP6401056B2 (ja) | 2012-04-27 | 2013-04-26 | フルクトシルヘキサペプチドに作用する改変型アマドリアーゼ |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2018186837A JP2018186837A (ja) | 2018-11-29 |
| JP2018186837A5 true JP2018186837A5 (https=) | 2019-06-27 |
| JP6726243B2 JP6726243B2 (ja) | 2020-07-22 |
Family
ID=49483330
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014512732A Active JP6401056B2 (ja) | 2012-04-27 | 2013-04-26 | フルクトシルヘキサペプチドに作用する改変型アマドリアーゼ |
| JP2018166687A Active JP6726243B2 (ja) | 2012-04-27 | 2018-09-06 | フルクトシルヘキサペプチドに作用する改変型アマドリアーゼ |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014512732A Active JP6401056B2 (ja) | 2012-04-27 | 2013-04-26 | フルクトシルヘキサペプチドに作用する改変型アマドリアーゼ |
Country Status (4)
| Country | Link |
|---|---|
| US (1) | US10767211B2 (https=) |
| EP (2) | EP3508577A3 (https=) |
| JP (2) | JP6401056B2 (https=) |
| WO (1) | WO2013162035A1 (https=) |
Families Citing this family (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2013162035A1 (ja) * | 2012-04-27 | 2013-10-31 | キッコーマン株式会社 | フルクトシルヘキサペプチドに作用する改変型アマドリアーゼ |
| JP6363327B2 (ja) * | 2013-03-25 | 2018-07-25 | キッコーマン株式会社 | 改変アマドリアーゼ |
| JP6328115B2 (ja) * | 2013-07-09 | 2018-05-23 | 協和メデックス株式会社 | 糖化ヘキサペプチドオキシダーゼとその利用 |
| ES2848705T3 (es) * | 2013-08-09 | 2021-08-11 | Kikkoman Corp | Amadoriasa modificada y método para producirla, agente para mejorar la resistencia a tensioactivos de la amadoriasa y composición para medir la HbA1c usando la misma |
| JP6542671B2 (ja) * | 2013-10-25 | 2019-07-10 | キッコーマン株式会社 | ヘモグロビンＡ１ｃの測定方法および測定キット |
| CN105683390B (zh) | 2013-10-25 | 2021-02-26 | 龟甲万株式会社 | 使用作用于糖基化肽的阿马多里酶的HbA1c测定方法 |
| EP3786291B1 (en) | 2014-10-24 | 2023-10-18 | Kikkoman Corporation | Amadoriase having enhanced dehydrogenase activity |
| WO2016072520A1 (ja) * | 2014-11-07 | 2016-05-12 | キッコーマン株式会社 | アニオン性界面活性剤耐性が向上したアマドリアーゼ |
| JP6764219B2 (ja) * | 2014-12-26 | 2020-09-30 | キッコーマン株式会社 | グッド緩衝液に対して安定なアマドリアーゼ |
| EP3279323B1 (en) | 2015-04-03 | 2023-03-08 | Kikkoman Corporation | Amadoriase having improved specific activity |
| KR102596402B1 (ko) * | 2016-04-22 | 2023-10-31 | 기꼬만 가부시키가이샤 | HbA1c 디히드로게나아제 |
| WO2018012607A1 (ja) | 2016-07-13 | 2018-01-18 | キッコーマン株式会社 | 反応促進剤 |
| JP7020413B2 (ja) | 2016-07-29 | 2022-02-16 | ミナリスメディカル株式会社 | 糖化ヘモグロビンの測定方法 |
| JP7157063B2 (ja) | 2017-08-31 | 2022-10-19 | キッコーマン株式会社 | 糖化ヘモグロビンオキシダーゼ改変体及び測定方法 |
| JP6818718B2 (ja) * | 2018-06-28 | 2021-01-20 | キッコーマン株式会社 | 改変アマドリアーゼ |
| CN112143825B (zh) * | 2020-09-28 | 2021-08-03 | 华南农业大学 | 一种区分检测花生黑腐病菌和花生基腐病菌的双重pcr检测引物及应用 |
Family Cites Families (25)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS61280297A (ja) | 1985-06-04 | 1986-12-10 | Noda Sangyo Kagaku Kenkyusho | アマドリ化合物の定量法及びその定量用試薬 |
| GB9116315D0 (en) | 1991-07-29 | 1991-09-11 | Genzyme Ltd | Assay |
| WO1997013872A1 (en) | 1995-10-12 | 1997-04-17 | Kyoto Daiichi Kagaku Co., Ltd. | Method and assaying amodori compounds |
| US6767701B1 (en) * | 1998-10-26 | 2004-07-27 | Novozymes A/S | Methods of constructing and screening a DNA library of interest in filamentous fungal cells |
| JP3949854B2 (ja) | 1999-10-01 | 2007-07-25 | キッコーマン株式会社 | 糖化蛋白質の測定方法 |
| JP4231668B2 (ja) | 2001-09-04 | 2009-03-04 | キッコーマン株式会社 | 新規なフルクトシルペプチドオキシダーゼ |
| DE60326259D1 (de) | 2002-10-23 | 2009-04-02 | Daiichi Pure Chemicals Co Ltd | Neue fructosylpeptidoxidase und deren nutzung |
| JP4227820B2 (ja) | 2003-03-12 | 2009-02-18 | 旭化成ファーマ株式会社 | 新規な酵素 |
| JP4248900B2 (ja) | 2003-03-14 | 2009-04-02 | イチビキ株式会社 | 新規なフルクトシルアミンオキシダーゼをコードする遺伝子及びそれを用いての該フルクトシルアミンオキシダーゼの製造方法 |
| WO2004104203A1 (ja) | 2003-05-21 | 2004-12-02 | Asahi Kasei Pharma Corporation | ヘモグロビンA1c測定法およびそれに用いる酵素とその製造法 |
| JP2005110657A (ja) | 2003-09-18 | 2005-04-28 | Kikkoman Corp | α−糖化ジペプチドの製造法及びα−糖化ジペプチドの測定法 |
| ES2363228T3 (es) | 2003-11-19 | 2011-07-27 | Sekisui Medical Co., Ltd. | Procedimiento de ensayo de proteína glicosilada. |
| JP5074386B2 (ja) | 2006-04-25 | 2012-11-14 | キッコーマン株式会社 | 熱安定性に優れた真核型アマドリアーゼ、その遺伝子及び組換え体ｄｎａ、並びに熱安定性に優れた真核型アマドリアーゼの製造法 |
| WO2008018094A1 (en) | 2006-08-07 | 2008-02-14 | Stmicroelectronics S.R.L. | Control device for power factor correction device in forced switching power supplies |
| WO2008108385A1 (ja) | 2007-03-05 | 2008-09-12 | Kikkoman Corporation | 糖化ヘキサペプチドの測定方法 |
| JP5243878B2 (ja) | 2008-08-04 | 2013-07-24 | 東洋紡株式会社 | フルクトシルバリルヒスチジン測定用酵素、およびその利用法 |
| JP5350762B2 (ja) | 2008-08-04 | 2013-11-27 | 東洋紡株式会社 | フルクトシルアミノ酸オキシダーゼ、およびその利用法 |
| KR20110069138A (ko) | 2008-10-09 | 2011-06-22 | 교와 메덱스 가부시키가이샤 | 신규 프럭토실펩티드옥시다아제 |
| CN102171338B (zh) | 2008-10-10 | 2014-08-13 | 东洋纺织株式会社 | 具有果糖基缬氨酰基组氨酸氧化酶活性的蛋白质及其修饰产物以及其应用 |
| JP5476021B2 (ja) * | 2008-10-17 | 2014-04-23 | 東洋紡株式会社 | フルクトシルアミノ酸オキシダーゼ改変体およびその利用 |
| EP2281900A1 (en) | 2009-08-03 | 2011-02-09 | Roche Diagnostics GmbH | Fructosyl peptidyl oxidase and sensor for assaying a glycated protein |
| EP2287295A1 (en) | 2009-08-03 | 2011-02-23 | Roche Diagnostics GmbH | Mutant Fructosyl amino acid oxidase |
| JP5927771B2 (ja) | 2010-04-09 | 2016-06-01 | 東洋紡株式会社 | ヘモグロビンＡ１ｃの測定方法 |
| WO2012018094A1 (ja) | 2010-08-06 | 2012-02-09 | キッコーマン株式会社 | 基質特異性が改変されたアマドリアーゼ |
| WO2013162035A1 (ja) * | 2012-04-27 | 2013-10-31 | キッコーマン株式会社 | フルクトシルヘキサペプチドに作用する改変型アマドリアーゼ |
-
2013
- 2013-04-26 WO PCT/JP2013/062508 patent/WO2013162035A1/ja not_active Ceased
- 2013-04-26 US US14/396,855 patent/US10767211B2/en active Active
- 2013-04-26 JP JP2014512732A patent/JP6401056B2/ja active Active
- 2013-04-26 EP EP19154807.2A patent/EP3508577A3/en active Pending
- 2013-04-26 EP EP13781492.7A patent/EP2843050B1/en active Active
-
2018
- 2018-09-06 JP JP2018166687A patent/JP6726243B2/ja active Active
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2018186837A5 (https=) | ||
| RU2012106148A (ru) | Вариантные формы уратоксидазы и их применение | |
| Svendsen et al. | Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis | |
| JP2022046503A5 (https=) | ||
| JP2017121261A5 (https=) | ||
| RU2007141683A (ru) | Вариантная форма урат-оксидазы и ее использование | |
| FI3256579T3 (fi) | Kysteiiniproteaasi | |
| JP2004267216A5 (https=) | ||
| JP2016523959A5 (https=) | ||
| JP2022188182A5 (https=) | ||
| CN110892067A (zh) | 热稳定性提高的phi29DNA聚合酶突变体 | |
| AU2004204031A1 (en) | Dimerized peptide | |
| JP2003530124A5 (https=) | ||
| DK2204450T3 (en) | alkaline proteases | |
| RU2018121480A (ru) | СПОСОБ ПОЛУЧЕНИЯ ХИМИЧЕСКИХ ПРОДУКТОВ ТОНКОГО СИНТЕЗА С ПОМОЩЬЮ CORYNEBACTERIUM, СЕКРЕТИРУЮЩЕЙ МОДИФИЦИРОВАННЫЕ a-1,6-ГЛЮКОЗИДАЗЫ | |
| RU2014144881A (ru) | Способ экспрессии полипептидов с применением модифицированных нуклеиновых кислот | |
| CA2158047A1 (en) | Allergenic protein and peptides from house dust mite and uses therefor | |
| RU2012121884A (ru) | Варианты вируса гепатита с | |
| KR102390400B1 (ko) | 당화 펩티드에 작용하는 아마도리아제를 이용한 HbA1c 측정법 | |
| WO2009020632A1 (en) | Znf206: a novel regulator of embryonic stem cell self-renewal and pluripotency | |
| CA2411694A1 (en) | Furin polypeptides with improved characteristics | |
| CHANG et al. | In vitro processing of proopiocortin by membrane-associated and soluble converting enzyme activities from rat intermediate lobe secretory granules | |
| CA2445700A1 (en) | Protein involved in restoration of cytoplasmic male sterility to fertility and gene encoding the protein and gene | |
| Haas et al. | Application of mass spectrometry to the analysis of proteins containing a N-terminal pyroglutamic acid residue | |
| JP2024118708A5 (https=) |