序号 专利名 申请号 申请日 公开(公告)号 公开(公告)日 发明人
1 重组杆状病毒及其应用 CN201410122911.1 2014-03-28 CN104073471A 2014-10-01 坂东孝彦; 菅井睦美
发明提供整合了编码γ-谷酰羧化酶(GGCX)的基因及编码DT-黄递酶(NQO1)的基因的重组杆状病毒。
2 利用稳定辅酶的酶的稳定化 CN201080036800.9 2010-08-18 CN102471767A 2012-05-23 W.勒德尔; C.霍恩; N.施泰因克; N.布西; T.迈尔; R.施姆克; R.纳格尔; D.海因德尔
发明涉及通过在存在稳定化的辅酶的情况下保存酶来使酶稳定的方法。此外,本发明涉及利用稳定化的辅酶来稳定化的酶,以及其在用于检测被分析物的测试元件中的用途。
3 蛋白质的纯化方法及含肽标签的融合蛋白质及其生产方法 CN201710199777.9 2017-03-30 CN107266523A 2017-10-20 髙桥亮
发明涉及蛋白质的纯化方法及含肽标签的融合蛋白质及其生产方法,更具体涉及包括调制包含含有含12个残基以上的酸性基酸残基的肽标签的氨基酸序列和目标蛋白质的氨基酸序列的融合蛋白质的试样的工序、及分离与上述融合蛋白质一同含在上述试样中的混杂蛋白质和上述试样中的融合蛋白质的工序的蛋白质的纯化方法。
4 COMPOSITIONS OF ENZYMES STABILIZED WITH STABLE COENZYMES US15363038 2016-11-29 US20170073661A1 2017-03-16 Wolfgang Roedel; Carina Horn; Nelli Steinke; Nadine Bucci; Thomas Meier; Rainer Schmuck; Rolf Nagel; Dieter Heindl
Methods are provided for stabilizing an enzyme by storing the enzyme in the presence of a stabilized coenzyme. In addition, enzymes are provided that are stabilized with a stabilized coenzyme, as well as the use thereof in test elements for detecting analytes. Other aspects include unique compositions, methods, techniques, systems and devices involving enzyme stabilization.
5 Stabilization of enzymes with stable coenzymes US13400209 2012-02-20 US09540702B2 2017-01-10 Wolfgang Roedel; Carina Horn; Nelli Steinke; Nadine Bucci; Thomas Meier; Rainer Schmuck; Rolf Nagel; Dieter Heindl
Methods for stabilizing an enzyme by storing the enzyme in the presence of a stabilized coenzyme are disclosed. In addition, an enzyme stabilized with a stabilized coenzyme as well as the use thereof in test elements for detecting analytes are also disclosed. Other aspects include unique compositions, methods, techniques, systems and devices involving enzyme stabilization.
6 METHOD FOR PURIFYING PROTEIN US15480881 2017-04-06 US20170291918A1 2017-10-12 Ryo TAKAHASHI
Disclosed is a method for purifying a protein, comprising steps of: preparing a sample containing a fusion protein containing an amino acid sequence of a peptide tag and an amino acid sequence of a target protein; and separating contaminant proteins contained with the fusion protein in the sample and the fusion protein in the sample, wherein the peptide tag contains 12 or more acidic amino acid residues.
7 Recombinant baculovirus and use thereof US14227747 2014-03-27 US09303251B2 2016-04-05 Takahiko Bando; Mutsumi Sugai
The present invention provides a recombinant baculovirus. The baculovirus has a genome into which a gene encoding γ-glutamyl carboxylase (GGCX) and a gene encoding DT-diaphorase (NQO1) are incorporated.The present invention further provides a method for producing a recombinant vitamin K-dependent protein by using the recombinant baculovirus.
8 RECOMBINANT BACULOVIRUS AND USE THEREOF US14227747 2014-03-27 US20140295496A1 2014-10-02 Takahiko BANDO; Mutsumi SUGAI
The present invention provides a recombinant baculovirus. The baculovirus has a genome into which a gene encoding γ-glutamyl carboxylase (GGCX) and a gene encoding DT-diaphorase (NQO1) are incorporated.The present invention further provides a method for producing a recombinant vitamin K-dependent protein by using the recombinant baculovirus.
9 METHOD FOR CONTROLLING NAD(P)/NAD(P)H RATIO BY OXIDOREDUCTASE US14135015 2013-12-19 US20140106387A1 2014-04-17 Myung-Gyu PARK; Sang-Ku YOO; In Geun JO; Taehwan KWAK
Provided is a method capable of effectively treating various diseases associated with energy excess, such as obesity, diabetes, metabolic syndromes, degenerative diseases and mitochondrial dysfunction-related diseases, via elevation of an NAD(P)+/NAD(P)H ratio by increasing an NAD(P)+ concentration in vivo or in vitro through use of NAD(P)H as a substrate or coenzyme by oxidoreductase such as NAD(P)H:quinone oxidoreductase (NQO1), a method of screening a drug for the same and a therapeutic drug.
10 STABILIZATION OF ENZYMES WITH STABLE COENZYMES US13400209 2012-02-20 US20120276565A1 2012-11-01 Wolfgang Roedel; Carina Horn; Nelli Steinke; Nadine Bucci; Thomas Meier; Rainer Schmuck; Rolf Nagel; Dieter Heindl
Methods for stabilizing an enzyme by storing the enzyme in the presence of a stabilized coenzyme are disclosed. In addition, an enzyme stabilized with a stabilized coenzyme as well as the use thereof in test elements for detecting analytes are also disclosed. Other aspects include unique compositions, methods, techniques, systems and devices involving enzyme stabilization.
11 METHOD FOR CONTROLLING NAD(P)/NAD(P)H RATIO BY OXIDOREDUCTASE US12162293 2007-02-15 US20090215145A1 2009-08-27 Myung-Gyu Park; Sang-Ku Yoo; In Geun Jo; Taehwan Kwak
Provided is a method capable of effectively treating various diseases associated with energy excess, such as obesity, diabetes, metabolic syndromes, degenerative diseases and mitochondrial dysfunction-related diseases, via elevation of an NAD(P)+/NAD(P)H ratio by increasing an NAD(P)+ concentration in vivo or in vitro through use of NAD(P)H as a substrate or coenzyme by oxidoreductase such as NAD(P)H:quinone oxidoreductase (NQO1), a method of screening a drug for the same and a therapeutic drug.
12 組換えバキュロウイルスおよびその利用 JP2013072021 2013-03-29 JP5830486B2 2015-12-09 坂東 孝彦; 菅井 睦美
13 METHOD FOR PURIFYING PROTEIN, FUSION PROTEIN CONTAINING PEPTIDE TAG, AND PRODUCTION METHOD THEREOF EP17165390.0 2017-04-07 EP3248984A2 2017-11-29 Takahashi, Ryo

Disclosed is a method for purifying a protein, comprising steps of: preparing a sample containing a fusion protein containing an amino acid sequence of a peptide tag and an amino acid sequence of a target protein; and separating contaminant proteins contained with the fusion protein in the sample and the fusion protein in the sample, wherein the peptide tag contains 12 or more acidic amino acid residues.

14 STABILISIERUNG VON ENZYMEN MIT STABILEN COENZYMEN EP10757053.3 2010-08-18 EP2467478B1 2015-09-16 RÖDEL, Wolfgang; HORN, Carina; STEINKE, Nelli; BUCCI, Nadine; MEIER, Thomas; SCHMUCK, Rainer; NAGEL, Rolf; HEINDL, Dieter
15 組換えバキュロウイルスおよびその利用 JP2013072021 2013-03-29 JP2014195411A 2014-10-16 BANDO TAKAHIKO; SUGAI MUTSUMI
【課題】ビタミンK依存性タンパク質を簡便かつ大量に製造可能であることと、得られたビタミンK依存性タンパク質が十分にγ−グルタミルカルボキシル化されていることとの両方の条件を満足する、組換え型ビタミンK依存性タンパク質を製造する手段を提供することを課題とする。【解決手段】γ−グルタミルカルボキシラーゼ(GGCX)をコードする遺伝子およびDT−ジアホラーゼ(NQO1)をコードする遺伝子が組み込まれた組換えバキュロウイルスを、鱗翅目昆虫またはこの昆虫の培養細胞を利用した発現系に用いることにより、上記の課題を解決する。【選択図】なし
16 Method for controlling nad by oxidoreductase (p) / nad (p) h ratio JP2008555159 2007-02-15 JP2009526839A 2009-07-23 カク,テファン; グン ジョ,イン; パク,ミュン−ギュ; ヨ,サン−ク
肥満、糖尿病、代謝症候群、変性疾患およびミトコンドリア機能障害に関連する疾患などのエネルギー過剰を伴う様々な疾患を、インビボまたはインビトロで、基質または補酵素としてNAD(P)Hの使用を通じて、NAD(P)H:キノンオキシドレダクターゼ(NQO1)などのオキシドレダクターゼによりNAD(P) 濃度を上昇させることによるNAD(P) /NAD(P)H比の上昇を介して有効に治療することが可能な方法と、それらに対する薬剤および治療薬のスクリーニング方法が提供される。
17 JPH03503761A - JP50376289 1989-02-22 JPH03503761A 1991-08-22
18 Recombinant baculovirus and use thereof EP14162163.1 2014-03-28 EP2784087B1 2017-03-01 Bando, Takahiko; Sugai, Mutsumi
19 Method for controlling NAD(P)/NAD(P)H ratio by oxidoreductase EP11179000.2 2007-02-15 EP2426212A1 2012-03-07 Park, Myung-Gyu; Yoo, Sang-Ku; Jo, In Geun; Kwak, Taehwan

The present invention provides a method capable of effectively treating various diseases associated with energy excess, such as obesity, diabetes, metabolic syndromes, degenerative diseases and mitochrondrial dysfunction-related diseases, via elevation of an NAD(P)+ZNAD(P)H ratio by increasing an NAD(P)+ concentration in vivo or in vitro through use of NAD(P)H as a substrate or coenzyme by oxidoreductase such as NAD(P)H:quinine oxidoreductase (NQO1), a method of screening a drug for the same and a therapeutic drug.

20 Improvements relating to the control of neoplastic tissue growth EP89301678.2 1989-02-22 EP0330432A1 1989-08-30 Roberts, John J.; Knox, Richard J.; Friedlos, Frank; JARMAN, Michael

Compounds of the general formula: wherein R is H, an acyl group or a hydrocarbyl group containing up to 6 carbon atoms, have cytotoxic activity against several tumours. The 4-hydroxylamino compound can be obtained directly from the corresponding 2,4-dinitro compound by selective chemical reduction or by the action of a nitroreductase obtainable from Walker tumour cells. The 2,4-dinitro compound is substantially devoid of cytotoxic activity except in relation to Walker tumour cells and hence can act as a prodrug in regimes where a prodrug is localised in vivo in the regions of a tumour to be treated and is then activated to the cytotoxic 4-hydroxylamino compound under the influence of the enzyme.

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