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KR960031608A - 바실러스-유래 트랜스글루타미나제 - Google Patents

바실러스-유래 트랜스글루타미나제 Download PDF

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KR960031608A
KR960031608A KR1019960003112A KR19960003112A KR960031608A KR 960031608 A KR960031608 A KR 960031608A KR 1019960003112 A KR1019960003112 A KR 1019960003112A KR 19960003112 A KR19960003112 A KR 19960003112A KR 960031608 A KR960031608 A KR 960031608A
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transglutaminase
bacillus
amino acid
dna
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KR100358824B1 (ko
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가쓰노리 고바야시
시게루 야마나카
기요시 미와
슌이치 스즈키
유즈루 에토
유코 다니타
겐조 요코제키
겐이치 하쉬구치
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이나모리 쥰스케
아지노모토 가부시키가이샤
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    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/10—Transferases (2.)
    • C12N9/1025—Acyltransferases (2.3)
    • C12N9/104—Aminoacyltransferases (2.3.2)
    • C12N9/1044—Protein-glutamine gamma-glutamyltransferase (2.3.2.13), i.e. transglutaminase or factor XIII
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
    • C—CHEMISTRY; METALLURGY
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    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/88—Lyases (4.)
    • C—CHEMISTRY; METALLURGY
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    • C12P21/00—Preparation of peptides or proteins
    • Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
    • Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
    • Y10S435/00—Chemistry: molecular biology and microbiology
    • Y10S435/8215—Microorganisms
    • Y10S435/822—Microorganisms using bacteria or actinomycetales
    • Y10S435/832—Bacillus
    • Y10S435/839—Bacillus subtilis

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Abstract

본 발명은 (1) 바실러스 섭틸리스(Bacillus subtilis)와 같은 바실러스에 의해 생산되는 트랜스글루타미나제(이하, TG라고 한다), (2) 트랜스글루타미나제 활성을 갖는 분획, (3) 단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체 중의 글루타민 및 리신 잔기를 TG 또는 TG 활성을 갖는 분획의 작용에 의해 가교 결합시킴으로서 단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체의 분자 사이에 또는 분자내에 분자간 또는 분자내 가교 결합된 ε-(r-Glu)-Lus 결합을 형성시킴을 특징으로 하는, 가교 결합된 구조를 갖는 단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체를 생산하는 방법에 관한 것이다.
본 발명은 또한, (4) 바실러스 섭틸리스 등의 바실러스로부터 유도된 트랜스글루타미나제를 코딩하는 DNA, (5) 벡터 DNA를 DNA에 연결시킴으로써 수득한 재조합 DNA, (6) 이 재조합 DNA로 형질전환시킨 세포, 및 (7)이 형질전환체를 배양시킴으로써 바실러스-유래 트랜스 글루타미나제를 생산하는 방법에 관한 것이다.

Description

바실러스-유래 트랜스글루타미나제
본 내용은 요부공개 건이므로 전문내용을 수록하지 않았음
제1도는 순수 TG-1의 SDS-PAGE의 결과를 도시한다,
제3도는 TG-1의 활성에 대한 온도 곡선을 도시한다,
제5도는 TG-1로 가교 결합된 α-카제인을 도시한다,
제7도는 TG-2의 활성에 대한 pH 곡선을 도시한다.

Claims (13)

1) 적합한 pH가 약 7 내지 약 9이고, 2) 적합한 온도가 약 40℃ 내지 약 65℃이며, 3) 약 60℃ 이하에서 안정하고, 4) Ca2+에 독립성이며, 5mM의 Ca2+존재하에서 50% 이상의 활성을 가지며, 5) NEM, 시스타민 및 (NH4)2SO4에 의해 억제되고, 6) EDTA, DTT 및 2-ME에 의해 억제되지 않으며, 7) (a) 겔 투과에 의해 측정한 분자량이 약 18,000 내지 약 22,000이고 (b) SDS-PAGE에 의해 측정한 분자량이 약 28,000 내지 약 30,000이며, 8) 펩티드 사슬 내에 존재하는 글루타민 잔기중의 γ-카르복시아미드 그룹의 트랜스아실화를 촉매화함을 특징으로 하는 바실러스-유래 트랜스글루타미나제.
제1항에 있어서, 서열 목록에 열거된 서열 번호 1의 아미노산 서열을 갖는 바실러스-유래 트랜스글루타미나제.
배양된 바실러스의 포자낭을 파열시키거나 용해함으로써 얻은 포자로부터 분획화시킨 바실러스-유래 트랜스글루타미나제 분획.
제1항에 있어서, 바실러스가 바실러스 섭틸리스(Bacillus subtilis)인 트랜스글루타미나제.
제3항에 있어서, 바실러스가 바실러스 섭틸리스인 트랜스글루타미나제 분획.
단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체 중의 글루타민 및 리신 잔기를 제1항의 트랜스글루타미나제의 작용에 의해 가교 결합시킴으로서 단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체의 분자 사이에 또는 분자 내에 분자간 또는 분자내 가교 결합된 ε-(r-Glu)-Lys 결합을 형성시킴을 특징으로 하는, 가교 결합된 구조를 갖는 단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체를 생산하는 방법.
단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체 중의 글루타민 및 리신 잔기를 제3항의 트랜스글루타미나제 분획의 작용에 의해 가교 결합시킴으로서 단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체의 분자 사이에 또는 분자내에 분자간 또는 분자내 가교 결합된 ε-(r-Glu)-Lys 결합을 형성시킴을 특징으로 하는, 가교 결합하다 구조를 갖는 단백질, 비단백질성 아미노산 중합체, 펩티드 또는 이들의 유도체를 생산하는 방법.
제1항의 트랜스글루타미나제를 코딩하는 DNA.
제8항에 있어서, 서열 목록에 열거된 서열 번호 2의 염기 서열 중의 적어도 118번째 염기 내지 852번째 염기의 서열을 갖는 DNA.
벡터 DNA를 제8항의 DNA에 연결시킴으로써 수득된 재조합 DNA.
제10항에 있어서, 재조합 DNA로 형질전환시킨 세포.
제11항의 세포를 배지 중에서 배양시킴으로써 바실러스-유래 트랜스글루타미나제를 배지 및/또는 세포중에 생산하여 축적시키고 이어서 트랜스글루타미나제를 수집하는 것을 특징으로 하는, 바실러스-유래 트랜스글루타미나제의 생산 방법.
제12항의 방법에 다라 생성된 바실러스-유래 트랜스글루타미나제.
※ 참고사항 : 최초출원 내용에 의하여 공개하는 것임.
KR1019960003112A 1995-02-09 1996-02-09 바실러스기원한트랜스글루타미나제 Expired - Fee Related KR100358824B1 (ko)

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JP2196395 1995-02-09
JP95-021963 1995-02-09
JP22631695 1995-09-04
JP95-226316 1995-09-04
JP96-013072 1996-01-29
JP01307296A JP3669390B2 (ja) 1995-02-09 1996-01-29 バチルス属細菌由来のトランスグルタミナーゼ

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KR960031608A true KR960031608A (ko) 1996-09-17
KR100358824B1 KR100358824B1 (ko) 2003-01-24

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US (2) US5731183A (ko)
EP (1) EP0726317B1 (ko)
JP (1) JP3669390B2 (ko)
KR (1) KR100358824B1 (ko)
AT (1) ATE361366T1 (ko)
AU (1) AU691714B2 (ko)
CA (1) CA2169249A1 (ko)
DE (1) DE69637054T2 (ko)
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Families Citing this family (60)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1996041866A1 (fr) 1995-06-08 1996-12-27 Ajinomoto Co., Inc. Procede microbien de production de transglutaminase
JP3635801B2 (ja) * 1996-08-01 2005-04-06 味の素株式会社 乳ホエイ蛋白含有粉末及びこれを使用した加工食品
EP0889133B1 (en) * 1997-07-04 2004-03-10 Ajinomoto Co., Inc. Process for producing microbial transglutaminase
US6821763B2 (en) * 1997-07-04 2004-11-23 Ajinomoto Co., Inc. Process for producing microbial transglutaminase
DE19732917C1 (de) * 1997-07-30 1998-10-15 Fuchsbauer Hans Lothar Verfahren zum Transglutaminase-katalysierten Koppeln von Protein oder Peptid an einen Träger
DE19814860A1 (de) * 1998-04-02 1999-10-07 Fuchsbauer Hans Lothar Bakterielle Transglutaminasen
AU4746100A (en) 1999-03-31 2000-10-16 Norbert Hampp Linker-free covalent coupling of bacteriorhodopsin in purple membrane form
US6093424A (en) * 1999-04-27 2000-07-25 Kraft Foods, Inc. Process for making cheese using transglutaminase and a non-rennet protease
US6251445B1 (en) 1999-05-19 2001-06-26 Kraft Foods, Inc. Method for producing enzyme-modified cheese flavorings
US6224914B1 (en) 1999-06-03 2001-05-01 Kraft Foods, Inc. Process for incorporating whey proteins into cheese using transglutaminase
US6270814B1 (en) 1999-06-03 2001-08-07 Kraft Foods, Inc. Incorporation of whey into process cheese
AU776775B2 (en) 1999-09-17 2004-09-23 Ajinomoto Co., Inc. Salting agent for food processing
KR20010078440A (ko) * 2001-01-11 2001-08-21 김형순,성문희 고분자량의 폴리-감마-글루탐산을 생산하는 내염성 균주바실러스 서브틸리스 청국장
US6416797B1 (en) 2001-02-14 2002-07-09 Kraft Foods Holdings, Inc. Process for making a wheyless cream cheese using transglutaminase
US6572901B2 (en) 2001-05-02 2003-06-03 Kraft Foods Holdings, Inc. Process for making a cheese product using transglutaminase
ES2223227B1 (es) * 2002-05-31 2006-04-16 Consejo Sup. Investig. Cientificas Secuencia de nucleotidos de maiz codificante de una proteina con actividad transglutaminasa, y su uso.
KR100399091B1 (en) * 2002-07-10 2003-09-22 Bioleaders Corp Macromolecular weight poly(gamma-glutamic acid) and its use
US7069233B2 (en) * 2002-12-31 2006-06-27 Bracken Foster & Associates, Llc System and method for identification and notification of elevated over-the-counter medication sales with response coordination
US6908634B2 (en) * 2003-03-20 2005-06-21 Solae, Llc Transglutaminase soy fish and meat products and analogs thereof
ES2397241T3 (es) 2004-01-21 2013-03-05 Novo Nordisk Health Care Ag Conjugación de péptidos mediante transglutaminasa
KR100517114B1 (ko) * 2005-02-25 2005-09-27 주식회사 바이오리더스 폴리감마글루탐산을 함유하는 면역보강제 조성물
CN101854960B (zh) 2006-12-15 2014-06-25 生命连结有限公司 明胶-转谷氨酰胺酶止血敷料和密封材料
JP2010539213A (ja) 2007-09-20 2010-12-16 ビーエーエスエフ ソシエタス・ヨーロピア 殺菌性株及び活性成分を含む組み合わせ
EP2310459B1 (en) 2008-06-18 2014-10-22 Lifebond Ltd Improved cross-linked compositions
US20110112573A1 (en) * 2008-06-18 2011-05-12 Orahn Preiss Bloom Methods and devices for use with sealants
US20110086014A1 (en) * 2008-06-18 2011-04-14 Ishay Attar Method for enzymatic cross-linking of a protein
EP2323694A1 (en) * 2008-08-06 2011-05-25 Novo Nordisk Health Care AG Conjugated proteins with prolonged in vivo efficacy
AU2010207725B2 (en) 2009-01-22 2015-06-11 Novo Nordisk Health Care Ag Stable growth hormone compounds
ES2401965T3 (es) 2009-02-19 2013-04-25 Novo Nordisk A/S Modificación de Factor VIII
GB0907323D0 (en) * 2009-04-29 2009-06-10 Dynea Oy Composite material comprising crosslinkable resin of proteinous material
US20100316764A1 (en) * 2009-06-10 2010-12-16 Engrain, LLC Flour supplement compositions and methods for preparing wheat flour
CN102612376A (zh) 2009-08-06 2012-07-25 诺沃-诺迪斯克保健股份有限公司 具有延长的体内功效的生长激素
US9066991B2 (en) 2009-12-22 2015-06-30 Lifebond Ltd. Modification of enzymatic crosslinkers for controlling properties of crosslinked matrices
JP5980689B2 (ja) 2010-01-22 2016-08-31 ノヴォ・ノルディスク・ヘルス・ケア・アーゲー 安定な成長ホルモン化合物
TWI508737B (zh) 2010-01-22 2015-11-21 諾佛 儂迪克股份有限公司 具有延長的活體內功效的生長激素
ITPD20100155A1 (it) 2010-05-19 2011-11-20 Univ Padova Metodo per la preparazione di coniugati mediante transglutaminasi
US8961544B2 (en) 2010-08-05 2015-02-24 Lifebond Ltd. Dry composition wound dressings and adhesives comprising gelatin and transglutaminase in a cross-linked matrix
CN101984052B (zh) * 2010-12-09 2012-09-26 江南大学 一种谷氨酰胺转胺酶的分离纯化方法
CN102146361B (zh) * 2011-02-01 2013-06-19 泰兴市一鸣生物制品有限公司 一种分离纯化谷氨酰胺转胺酶的方法
FI126431B (fi) * 2011-06-16 2016-11-30 Valio Oy Juusto ja sen valmistus
EP2793947B1 (en) 2011-12-23 2021-02-03 Innate Pharma Enzymatic conjugation of polypeptides
EP2872894B1 (en) 2012-07-13 2019-04-17 Innate Pharma Screening of conjugated antibodies
US10036010B2 (en) 2012-11-09 2018-07-31 Innate Pharma Recognition tags for TGase-mediated conjugation
WO2014140300A1 (en) 2013-03-15 2014-09-18 Innate Pharma Solid phase tgase-mediated conjugation of antibodies
ES2841123T3 (es) 2013-04-05 2021-07-07 Formulacion Del Compuesto De La Hormona De Crecimiento Formulación del compuesto de la hormona de crecimiento
WO2014202773A1 (en) 2013-06-20 2014-12-24 Innate Pharma Enzymatic conjugation of polypeptides
CN105517577A (zh) 2013-06-21 2016-04-20 先天制药公司 多肽的酶促偶联
CN105593238B (zh) 2013-07-11 2020-09-08 诺华股份有限公司 使用微生物转谷氨酰胺酶进行赖氨酸特异性化学酶法蛋白质修饰
CN113332449B (zh) 2014-06-12 2023-12-22 石药集团巨石生物制药有限公司 酶法制备同质的抗体-药物缀合物
CN105754892B (zh) * 2016-02-01 2019-09-06 华东师范大学 一种微生物谷氨酰胺转氨酶的分离纯化方法
EP3419670A2 (en) 2016-02-26 2019-01-02 Regeneron Pharmaceuticals, Inc. Optimized transglutaminase site-specific antibody conjugation
ES2896749T3 (es) 2016-05-13 2022-02-25 Rockwool Int Método para proporcionar aislamiento a una estructura
WO2019092148A1 (en) 2017-11-10 2019-05-16 Innate Pharma Antibodies with functionalized glutamine residues
US11998654B2 (en) 2018-07-12 2024-06-04 Bard Shannon Limited Securing implants and medical devices
CN111349594A (zh) * 2018-12-21 2020-06-30 南京百斯杰生物工程有限公司 一株能够生产谷氨酰胺转氨酶的菌株
US20220324932A1 (en) 2019-06-20 2022-10-13 CSPC Megalith Biopharmaceutical Co., Ltd. Modified il-2 proteins, peg conjugates, and uses thereof
MX2024010267A (es) 2022-02-22 2024-08-28 Adc Therapeutics Sa Método de conjugación que incluye una transglutaminasa en la región fc que comprende un n-glicano recortado.
EP4541376A1 (en) 2023-10-17 2025-04-23 ADC Therapeutics SA Antibody-drug conjugates
CN117063780B (zh) * 2023-10-17 2023-12-26 四川朕源生物科技有限公司 一种冬虫夏草子囊孢子采收培养基及其采收方法
WO2025120040A1 (en) 2023-12-06 2025-06-12 Adc Therapeutics Sa Anti-psma antibody drug conjugates comprising exatecan

Family Cites Families (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH0665280B2 (ja) * 1987-03-04 1994-08-24 味の素株式会社 タンパクゲル化剤及びそれを用いるタンパクのゲル化方法
DE69116495T2 (de) * 1990-10-19 1996-06-13 Ajinomoto Kk Rekombinante Transglutaminase
DE69533606T2 (de) * 1994-01-28 2006-03-02 Ajinomoto Co., Inc. Transglutaminase aus japanischer auster
EP0777726B1 (en) * 1994-08-26 2006-06-07 Novozymes A/S Microbial transglutaminases, their production and use

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