DK175569B1 - Rekombinant DNA-molekyle, fremgangsmåde til fremstilling deraf, transformeret vært indeholdende det rekombinante DNA-molekyle, fremgangsmåde til fremstilling af den transformerede vært samt fremgangsmåde til fremstilling af et polypeptid - Google Patents

Rekombinant DNA-molekyle, fremgangsmåde til fremstilling deraf, transformeret vært indeholdende det rekombinante DNA-molekyle, fremgangsmåde til fremstilling af den transformerede vært samt fremgangsmåde til fremstilling af et polypeptid Download PDF

Info

Publication number: DK175569B1
Authority: DK; Denmark
Prior art keywords: dna; recombinant dna; dna molecule; pli; gene
Prior art date: 1987-02-04

Application number

DK198800545A

Other languages

Danish (da)

English (en)

Other versions

DK54588A (da

DK54588D0 (da

Inventor

Jutta Heim

Jacob Visser

Christof Gysler

Hermanus Cornelius Mari Kester

Original Assignee

Novartis Ag

Priority date (The priority date 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 date listed.)

1987-02-04

Filing date

1988-02-03

Publication date

2004-12-13

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=10611694&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=DK175569(B1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1988-02-03 Application filed by Novartis Ag filed Critical Novartis Ag

1988-02-03 Publication of DK54588D0 publication Critical patent/DK54588D0/da

1988-08-05 Publication of DK54588A publication Critical patent/DK54588A/da

2004-12-13 Application granted granted Critical

2004-12-13 Publication of DK175569B1 publication Critical patent/DK175569B1/da

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DK198800545A 1987-02-04 1988-02-03 Rekombinant DNA-molekyle, fremgangsmåde til fremstilling deraf, transformeret vært indeholdende det rekombinante DNA-molekyle, fremgangsmåde til fremstilling af den transformerede vært samt fremgangsmåde til fremstilling af et polypeptid DK175569B1 (da)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
GB8702475		1987-02-04
GB878702475A GB8702475D0 (en)	1987-02-04	1987-02-04	Expression system

Publications (3)

Publication Number	Publication Date
DK54588D0 DK54588D0 (da)	1988-02-03
DK54588A DK54588A (da)	1988-08-05
DK175569B1 true DK175569B1 (da)	2004-12-13

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ID=10611694

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Application Number	Title	Priority Date	Filing Date
DK198800545A DK175569B1 (da)	1987-02-04	1988-02-03	Rekombinant DNA-molekyle, fremgangsmåde til fremstilling deraf, transformeret vært indeholdende det rekombinante DNA-molekyle, fremgangsmåde til fremstilling af den transformerede vært samt fremgangsmåde til fremstilling af et polypeptid

Country Status (23)

Country	Link
EP (2)	EP0278355B2 (de)
JP (1)	JP2633885B2 (de)
KR (1)	KR970001116B1 (de)
AT (1)	ATE133706T1 (de)
AU (1)	AU625773B2 (de)
CA (1)	CA1327330C (de)
DD (3)	DD283838A5 (de)
DE (1)	DE3854947T3 (de)
DK (1)	DK175569B1 (de)
ES (1)	ES2082746T5 (de)
FI (1)	FI105484B (de)
GB (1)	GB8702475D0 (de)
GR (1)	GR3018863T3 (de)
HU (1)	HU214005B (de)
IE (2)	IE72506B1 (de)
IL (1)	IL85293A (de)
MX (1)	MX10286A (de)
NO (1)	NO179078C (de)
NZ (1)	NZ223392A (de)
PH (1)	PH26106A (de)
PT (1)	PT86684B (de)
YU (1)	YU21688A (de)
ZA (1)	ZA88757B (de)

Families Citing this family (19)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5576195A (en) *	1985-11-01	1996-11-19	Xoma Corporation	Vectors with pectate lyase signal sequence
US5618920A (en) *	1985-11-01	1997-04-08	Xoma Corporation	Modular assembly of antibody genes, antibodies prepared thereby and use
US5447862A (en) *	1987-02-04	1995-09-05	Ciba-Geigy Corporation	Pectin lyase genes of aspergillus niger
EP0396612B1 (de) *	1988-01-11	1996-07-24	Xoma Corporation	Plasmidvektor mit pectatlyase-signalsequenz
AU627443B2 (en) *	1988-01-11	1992-08-27	Xoma Corporation	Novel plasmid vector with pectate lyase signal sequence
ES2063162T5 (es) *	1988-07-28	2002-11-16	Novartis Ag	Nuevo sistema de expresion.
EP0421919A3 (en) *	1989-09-02	1992-04-15	Ciba-Geigy Ag	Polygalacturonase encoding fungal expression system
PL175670B1 (pl) *	1992-12-24	1999-01-29	Gist Brocades Nv	Oczyszczona i wyizolowana sekwencja DNA kodująca polipeptyd wykazujący aktywność enzymu poligalakturonazy (PGX) z Aspergillus tubigensis
EP0688359A1 (de) *	1993-02-16	1995-12-27	Novo Nordisk A/S	Ein enzym mit pectinlyaseaktivität
US5674728A (en) *	1993-11-03	1997-10-07	Novartis Corporation	Aspergillus niger vacuolar aspartyl protease
AU2660397A (en) *	1996-04-05	1997-10-29	Board Of Regents, The University Of Texas System	Methods for producing soluble, biologically-active disulfide bond-containing eukaryotic proteins in bacterial cells
US6083715A (en) *	1997-06-09	2000-07-04	Board Of Regents, The University Of Texas System	Methods for producing heterologous disulfide bond-containing polypeptides in bacterial cells
US6165769A (en) *	1997-11-24	2000-12-26	Novo Nordisk A/S	Pectin degrading enzymes from Bacillus licheniformis
US6187580B1 (en)	1997-11-24	2001-02-13	Novo Nordisk A/S	Pectate lyases
WO1999027083A1 (en) *	1997-11-24	1999-06-03	Novo Nordisk A/S	PECTIN DEGRADING ENZYMES FROM $i(BACILLUS LICHENIFORMIS)
EP1187925B1 (de) *	1999-06-02	2005-03-30	Novozymes A/S	Pektat lyase-fusion zur expression und ausscheidung von polypeptiden
WO2010070146A1 (en)	2008-12-19	2010-06-24	Danisco A/S	Process for production of an enzyme product
AU2013302535B2 (en)	2012-08-16	2018-12-06	Bangladesh Jute Research Institute	Pectin degrading enzymes from Macrophomina phaseolina and uses thereof
WO2023225459A2 (en)	2022-05-14	2023-11-23	Novozymes A/S	Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4885249A (en)	1984-12-05	1989-12-05	Allelix, Inc.	Aspergillus niger transformation system
AU606033B2 (en)	1985-04-15	1991-01-31	Dsm Ip Assets B.V.	Promotors of filamentous fungi and use thereof
ES2063162T5 (es) *	1988-07-28	2002-11-16	Novartis Ag	Nuevo sistema de expresion.

1987
- 1987-02-04 GB GB878702475A patent/GB8702475D0/en active Pending
1988
- 1988-02-01 ES ES88101397T patent/ES2082746T5/es not_active Expired - Lifetime
- 1988-02-01 EP EP88101397A patent/EP0278355B2/de not_active Expired - Lifetime
- 1988-02-01 FI FI880439A patent/FI105484B/fi active IP Right Grant
- 1988-02-01 AT AT88101397T patent/ATE133706T1/de not_active IP Right Cessation
- 1988-02-01 DE DE3854947T patent/DE3854947T3/de not_active Expired - Lifetime
- 1988-02-01 EP EP95110254A patent/EP0683228A3/de not_active Withdrawn
- 1988-02-02 IL IL85293A patent/IL85293A/xx not_active IP Right Cessation
- 1988-02-02 CA CA000558001A patent/CA1327330C/en not_active Expired - Lifetime
- 1988-02-02 MX MX1028688A patent/MX10286A/es unknown
- 1988-02-02 PT PT86684A patent/PT86684B/pt not_active IP Right Cessation
- 1988-02-02 NZ NZ223392A patent/NZ223392A/en unknown
- 1988-02-03 DK DK198800545A patent/DK175569B1/da not_active IP Right Cessation
- 1988-02-03 IE IE29288A patent/IE72506B1/en not_active IP Right Cessation
- 1988-02-03 DD DD88327826A patent/DD283838A5/de not_active IP Right Cessation
- 1988-02-03 YU YU00216/88A patent/YU21688A/xx unknown
- 1988-02-03 JP JP63022134A patent/JP2633885B2/ja not_active Expired - Lifetime
- 1988-02-03 ZA ZA880757A patent/ZA88757B/xx unknown
- 1988-02-03 HU HU88508A patent/HU214005B/hu unknown
- 1988-02-03 DD DD31263288A patent/DD267511A5/de not_active IP Right Cessation
- 1988-02-03 IE IE960902A patent/IE960902L/xx not_active IP Right Cessation
- 1988-02-03 DD DD88327825A patent/DD283837A5/de not_active IP Right Cessation
- 1988-02-03 AU AU11234/88A patent/AU625773B2/en not_active Expired
- 1988-02-03 NO NO880470A patent/NO179078C/no not_active IP Right Cessation
- 1988-02-03 PH PH36456A patent/PH26106A/en unknown
- 1988-02-04 KR KR88001000A patent/KR970001116B1/ko not_active Expired - Lifetime
1996
- 1996-02-01 GR GR960400220T patent/GR3018863T3/el unknown

Also Published As

Publication number	Publication date
YU21688A (en)	1991-04-30
HU214005B (hu)	1998-08-28
DE3854947T3 (de)	2003-04-30
FI105484B (fi)	2000-08-31
DD283838A5 (de)	1990-10-24
GB8702475D0 (en)	1987-03-11
ZA88757B (en)	1988-08-04
EP0683228A2 (de)	1995-11-22
DE3854947T2 (de)	1996-11-14
NO179078B (no)	1996-04-22
AU625773B2 (en)	1992-07-16
FI880439A0 (fi)	1988-02-01
NZ223392A (en)	1991-05-28
PT86684B (pt)	1992-04-30
NO179078C (no)	1996-07-31
ATE133706T1 (de)	1996-02-15
EP0278355B1 (de)	1996-01-31
JPS63273480A (ja)	1988-11-10
PH26106A (en)	1992-02-06
IE72506B1 (en)	1997-04-23
IE960902L (en)	1988-08-04
DK54588A (da)	1988-08-05
CA1327330C (en)	1994-03-01
KR880010126A (ko)	1988-10-07
NO880470L (no)	1988-08-05
DE3854947D1 (de)	1996-03-14
NO880470D0 (no)	1988-02-03
MX10286A (es)	1993-12-01
ES2082746T3 (es)	1996-04-01
DK54588D0 (da)	1988-02-03
EP0278355A2 (de)	1988-08-17
EP0278355B2 (de)	2002-10-23
GR3018863T3 (en)	1996-05-31
IL85293A0 (en)	1988-07-31
JP2633885B2 (ja)	1997-07-23
AU1123488A (en)	1988-08-18
IE880292L (en)	1988-08-04
DD283837A5 (de)	1990-10-24
ES2082746T5 (es)	2003-06-16
EP0278355A3 (en)	1989-12-20
PT86684A (pt)	1988-03-01
EP0683228A3 (de)	1996-03-06
HUT46357A (en)	1988-10-28
DD267511A5 (de)	1989-05-03
IL85293A (en)	1992-12-01
FI880439L (fi)	1988-08-05
KR970001116B1 (en)	1997-01-28

Publication	Publication Date	Title
DK175569B1 (da)	2004-12-13	Rekombinant DNA-molekyle, fremgangsmåde til fremstilling deraf, transformeret vært indeholdende det rekombinante DNA-molekyle, fremgangsmåde til fremstilling af den transformerede vært samt fremgangsmåde til fremstilling af et polypeptid
DK173699B1 (da)	2001-07-02	Fremgangsmåde til fremstilling af en stamme af gæren Kluyveromyces, fremgangsmåde til fremstilling af et polypeptid i Kluyveromyces, anvendelse af Kluyveromyces som vært, transformet Kluyveromyces-celle og Kluyveromyces-ekspressionsvektor, samt plasmider
JP4307563B2 (ja)	2009-08-05	糸状菌、特にアスペルギルス属に属する糸状菌のアグロバクテリウム媒介性形質転換
FI104497B (fi)	2000-02-15	DNA-sekvenssi, joka koodittaa hiivan alkoholioksidaasi II:n säätelyaluetta
US4816405A (en)	1989-03-28	Vectors for transformation by ascomycetes
Herreros et al.	1992	A reorganized Candida albicans DNA sequence promoting homologous non‐integrative genetic transformation
EP0353188B1 (de)	1994-03-16	Expressionssystem
NO315330B1 (no)	2003-08-18	Isolert DNA-molekyl, hybridvektor omfattende denne, Aspergillusstamme defisient i et A. niger asparaginproteasegen, A. niger protease og entransformert vert samt fremgangsmater for a fremstille de ulike elementene
US5447862A (en)	1995-09-05	Pectin lyase genes of aspergillus niger
Picknett et al.	1987	Development of a gene transfer system for Penicillium chrysogenum
EP1040197A1 (de)	2000-10-04	Verfahren zur ortsspezifischen integration von mehrfachkopien eines gens in einem schimmelpilz
IL95553A (en)	2005-12-18	Recombinant dna molecules comprising a dna sequence from aspergillus niger and process for their preparation
CA1335081C (en)	1995-04-04	Expression system comprising aspergillus niger pectin lyase i gene sequences
KR0166956B1 (ko)	1999-01-15	펙틴 리아제의 발현 시스템을 암호화하는 재조합 dna분자
JPH0832241B2 (ja)	1996-03-29	新規遺伝子、ベクター、それを用いた形質転換体、及びその利用
CS270703B1 (cs)	1990-07-12	Způsob sekreční produkce cizorodých proteinů kultivací transformovaných kvasinkových buněk

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2008-02-18	PUP	Patent expired