AU6599386A - Creation of Inventions and Patents with Artificial Intelligence

AU6599386A – Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in
– Google Patents

AU6599386A – Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in
– Google Patents
Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in

Info

Publication number
AU6599386A

AU6599386A
AU65993/86A
AU6599386A
AU6599386A
AU 6599386 A
AU6599386 A
AU 6599386A
AU 65993/86 A
AU65993/86 A
AU 65993/86A
AU 6599386 A
AU6599386 A
AU 6599386A
AU 6599386 A
AU6599386 A
AU 6599386A
Authority
AU
Australia
Prior art keywords
pref
expression
esp
activation
denaturing
Prior art date
1985-10-23
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

Application number
AU65993/86A
Other versions

AU590029B2
(en

Inventor
Stephan Fischer
Ralf Mattes
Rainer Rudolph
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Roche Diagnostics GmbH

Original Assignee
Boehringer Mannheim GmbH
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.)
1985-10-23
Filing date
1986-10-23
Publication date
1987-05-19

1986-10-23
Application filed by Boehringer Mannheim GmbH
filed
Critical
Boehringer Mannheim GmbH

1987-05-19
Publication of AU6599386A
publication
Critical
patent/AU6599386A/en

1989-10-26
Application granted
granted
Critical

1989-10-26
Publication of AU590029B2
publication
Critical
patent/AU590029B2/en

2006-10-23
Anticipated expiration
legal-status
Critical

Status
Ceased
legal-status
Critical
Current

Links

Espacenet

Global Dossier

Discuss

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

C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals

C12N9/6424—Serine endopeptidases (3.4.21)

C12N9/6456—Plasminogen activators

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

C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals

C12N9/6424—Serine endopeptidases (3.4.21)

C12N9/6456—Plasminogen activators

C12N9/6459—Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA

C—CHEMISTRY; METALLURGY

C07—ORGANIC CHEMISTRY

C07K—PEPTIDES

C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length

C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides

C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure

C07K1/1133—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by redox-reactions involving cystein/cystin side chains

C—CHEMISTRY; METALLURGY

C07—ORGANIC CHEMISTRY

C07K—PEPTIDES

C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof

C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans

C07K14/52—Cytokines; Lymphokines; Interferons

C07K14/555—Interferons [IFN]

C07K14/565—IFN-beta

C—CHEMISTRY; METALLURGY

C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING

C12Y—ENZYMES

C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)

C12Y304/21—Serine endopeptidases (3.4.21)

C12Y304/21069—Protein C activated (3.4.21.69)

Abstract

Method for activating non-glycosylated tissue plasminogen activator (t-PA) after its expression in prokaryotic cells comprises cell lysis; solubilisation under denaturing and reducing conditions, and reactivation under oxidising conditions in presence of reduced and oxidised glutathione (G5H, G55G). The new feature is that in the last stage is at pH 9-12 (pref. 9.5-11) with G5H and G55G concns. 0.1-20, pref. 0.2-10, mM and 0.01-3, pref. 0.5-1, mM, respectively, and with a non-denaturing concn. of the denaturing agent. Esp. the method is applied to t-PA expressed in E.coli and P. putida. The denaturing agent is pref. arginine, guanidine hydrochloride (both at 0.1-1, esp. 0.25-0.75, mM) or urea, at 0.5-4 (esp. 1-3.5) M in the last stage.

AU65993/86A
1985-10-23
1986-10-23
Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in

Ceased

AU590029B2
(en)

Applications Claiming Priority (2)

Application Number
Priority Date
Filing Date
Title

DE19853537708

DE3537708A1
(en)

1985-10-23
1985-10-23

METHOD FOR ACTIVATING T-PA AFTER EXPRESSION IN PROKARYONTS

DE3537708

1985-10-23

Related Child Applications (1)

Application Number
Title
Priority Date
Filing Date

AU41321/89A
Division

AU607083B2
(en)

1985-10-23
1989-09-13
Process for the activation of genetically engineered, heterologous, disulphide bridge-containing eukaryotic proteins after expression in prokaryotes

Publications (2)

Publication Number
Publication Date

AU6599386A
true

AU6599386A
(en)

1987-05-19

AU590029B2

AU590029B2
(en)

1989-10-26

Family
ID=6284269
Family Applications (2)

Application Number
Title
Priority Date
Filing Date

AU65993/86A
Ceased

AU590029B2
(en)

1985-10-23
1986-10-23
Process for the activation of genetically engineered, heterologous disulfide bridge-containing eukaryotic proteins after expression in

AU41321/89A
Expired

AU607083B2
(en)

1985-10-23
1989-09-13
Process for the activation of genetically engineered, heterologous, disulphide bridge-containing eukaryotic proteins after expression in prokaryotes

Family Applications After (1)

Application Number
Title
Priority Date
Filing Date

AU41321/89A
Expired

AU607083B2
(en)

1985-10-23
1989-09-13
Process for the activation of genetically engineered, heterologous, disulphide bridge-containing eukaryotic proteins after expression in prokaryotes

Country Status (26)

Country
Link

EP
(3)

EP0253823A1
(en)

JP
(2)

JPH0728745B2
(en)

KR
(1)

KR900009139B1
(en)

AT
(2)

ATE131489T1
(en)

AU
(2)

AU590029B2
(en)

CA
(1)

CA1329157C
(en)

CZ
(1)

CZ280727B6
(en)

DD
(1)

DD260517A5
(en)

DE
(3)

DE3537708A1
(en)

DK
(2)

DK175091B1
(en)

ES
(2)

ES2061434T3
(en)

FI
(2)

FI94050C
(en)

GR
(2)

GR920300062T1
(en)

HK
(2)

HK153596A
(en)

HR
(1)

HRP921075B1
(en)

HU
(2)

HU204855B
(en)

IE
(1)

IE62634B1
(en)

IL
(1)

IL80325A
(en)

PT
(1)

PT83609B
(en)

SI
(1)

SI8611796B
(en)

SK
(1)

SK278317B6
(en)

SU
(1)

SU1607689A3
(en)

UA
(1)

UA6023A1
(en)

WO
(1)

WO1987002673A2
(en)

YU
(1)

YU47185B
(en)

ZA
(1)

ZA868012B
(en)

Cited By (3)

* Cited by examiner, † Cited by third party

Publication number
Priority date
Publication date
Assignee
Title

AU602664B2
(en)

1985-11-27
1990-10-25
Mitsui Toatsu Chemicals Inc.
DNA sequence containing the DNA sequence coding for human tissue plasminogen activator originating from human normal cells, recombinant DNA incorporating the DNA sequence, host cells transformed with the recombinant DNA, and process for producing human tissue plasminogen activator by use of the host cells

AU609645B2
(en)

1988-10-17
1991-05-02
Boehringer Mannheim Gmbh
Process for the activation of gene-technologically produced, biologically-active proteins expressed in prokaryotes

WO1992004382A1
(en)

1990-09-05
1992-03-19
Bunge (Australia) Pty. Ltd.
Solubilization of proteins in active forms

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Publication date
Assignee
Title

US4766205A
(en)

1985-11-13
1988-08-23
Beatrice Companies, Inc.
Method for isolation of recombinant polypeptides in biologically active forms

US4777043A
(en)

1985-12-17
1988-10-11
Genentech, Inc.
Stabilized human tissue plasminogen activator compositions

AU621051B2
(en)

1987-04-28
1992-03-05
Amgen, Inc.
Method for purifying granulocyte-macrophage colony stimulating factor

DE3722082A1
(en)

1987-07-03
1989-01-12
Behringwerke Ag

METHOD FOR DETERMINING THE ACTIVITY OF SERINE PROTEASES OR SERINE PROTEASE INHIBITORS

CA1340586C
(en)

1988-09-23
1999-06-08
Cetus Corporation
Process for recovering microbially produced interferon-beta

DE3832898A1
(en)

1988-09-28
1990-04-12
Boehringer Mannheim Gmbh

PRAEPARATE OF EXPRESSED PLASMINOGEN ACTIVATOR IN PROKARYONS

DE3903581A1
(en)

1989-02-07
1990-08-16
Boehringer Mannheim Gmbh

FABRIC PLASMINOGEN ACTIVATOR DERIVATIVE

DE3942143A1
(en)

1989-12-20
1991-06-27
Boehringer Mannheim Gmbh

T-PA PRO STABILIZATION

DE69126434D1
(en)

1990-08-20
1997-07-10
Novo Nordisk As

Process for the production of biologically active IGF-1 by using amino-terminally extended IGF-1

DE4037196A1
(en)

1990-11-22
1992-05-27
Boehringer Mannheim Gmbh

METHOD FOR REACTIVATING DENATURED PROTEIN

DE4113750A1
(en)

1991-04-26
1992-10-29
Boehringer Mannheim Gmbh

IMPROVEMENT OF RENATURATION IN THE SECRETION OF DISULFID-BRIDGED PROTEINS

DE4139000A1
(en)

1991-11-27
1993-06-03
Boehringer Mannheim Gmbh

METHOD OF GENERATING BIOLOGICALLY ACTIVE SS-NGF

US5212091A
(en)

1992-03-02
1993-05-18
Monsanto Company
Method of producing tissue factor pathway inhibitor

EP0586667A1
(en)

1992-03-24
1994-03-16
Synergen, Inc.
Refolding and purification of insulin-like growth factor i

DE59305396D1
(en)

1992-12-02
1997-03-20
Hoechst Ag

Process for obtaining proinsulin with correctly connected cystine bridges

DE4405179A1
(en)

1994-02-18
1995-08-24
Hoechst Ag

Method of obtaining insulin with correctly connected cystine bridges

FR2729972B1
(en)

1995-01-31
1997-04-18
Sanofi Sa

PROCESS FOR THE EXTRACTION OF PERIPLASMIC PROTEINS FROM PROKARYOTIC MICROORGANISMS IN THE PRESENCE OF ARGININ

US5714371A
(en)

1995-05-12
1998-02-03
Schering Corporation
Method for refolding insoluble aggregates of hepatitis C virus protease

US5728804A
(en)

1995-06-02
1998-03-17
Research Corporation Technologies, Inc.
Use of cyclodextrins for protein renaturation

US6342585B1
(en)

1996-06-11
2002-01-29
Roche Diagnostics Gmbh
Method of activating denatured protein

US7153943B2
(en)

1997-07-14
2006-12-26
Bolder Biotechnology, Inc.
Derivatives of growth hormone and related proteins, and methods of use thereof

US6653098B1
(en)

1998-02-23
2003-11-25
G. D. Searle & Co.
Method of producing mouse and human endostatin

DE19850429A1
(en)

1998-10-27
2000-05-04
Andre Schrattenholz

Fragments

EP1048732A1
(en)

1999-04-26
2000-11-02
F. Hoffmann-La Roche Ag
Process for producing natural folded and secreted proteins

EP1077263A1
(en)

1999-07-29
2001-02-21
F.Hoffmann-La Roche Ag
Process for producing natural folded and secreted proteins by co-secretion of chaperones

CN1318443C
(en)

2000-05-16
2007-05-30
博尔德生物技术公司
Methods for refolding proteins containing free cysteine residues

DE10105911A1
(en)

2001-02-09
2002-08-14
Roche Diagnostics Gmbh

Expression of the recombinant proteinase K from Tritirachium album in yeast

DE10105912A1
(en)

2001-02-09
2002-08-14
Roche Diagnostics Gmbh

Recombinant Proteinase K

DE102005033250A1
(en)

2005-07-15
2007-01-18
Bioceuticals Arzneimittel Ag

Process for purifying G-CSF

DE202006020194U1
(en)

2006-03-01
2007-12-06
Bioceuticals Arzneimittel Ag

G-CSF liquid formulation

AR062069A1
(en)

2006-07-14
2008-10-15
Genentech Inc

REPLEGED OF RECOMBINANT PROTEINS

US8617531B2
(en)

2006-12-14
2013-12-31
Bolder Biotechnology, Inc.
Methods of making proteins and peptides containing a single free cysteine

EA022821B1
(en)

2010-03-17
2016-03-31
Ратиофарм Гмбх
Method for obtaining biologically active recombinant human g-csf

JP2013540157A
(en)

2010-10-20
2013-10-31
メディミューン，エルエルシー

Method for treating inclusion bodies

HU1200171A1
(en)

2012-03-19
2013-09-30
Richter Gedeon Nyrt
Methods for the production of polypeptides

HU1200172A2
(en)

2012-03-19
2013-10-28
Richter Gedeon Nyrt
Methods for refolding g-csf from inclusion bodies

CN103852527B
(en)

2012-12-05
2015-05-13
中国科学院大连化学物理研究所
High-flux protein sample pre-treatment device

US10457716B2
(en)

2014-08-06
2019-10-29
University Of Notre Dame Du Lac
Protein folding and methods of using same

CA3044371A1
(en)

2016-12-30
2018-07-05
Biogend Therapeutics Co., Ltd.
Recombinant polypeptides and nucleic acid molecules, compositions, and methods of making and uses thereof

WO2022129460A1
(en)

2020-12-18
2022-06-23
Richter Gedeon Nyrt.
Methods for the purification of refolded fc-peptide fusion protein

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(en)

1974-09-18
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Fujiwa Kako Kk

KOJUNDOHITOROKINAAZE NO SEIHO

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(en)

1982-04-28
1984-08-28
The Bendix Corporation
Adjustable microwave power combiner for a plurality of coaxially mounted impatt diodes

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1984-02-21
Hoffmann-La Roche Inc.
Monomeric interferons

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Genentech Inc

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(en)

1983-03-25
1994-07-15
Celltech Ltd

METHOD OF PRODUCING A PROTEIN.

JPS6051119A
(en)

1983-08-30
1985-03-22
Green Cross Corp:The
Dried pharmaceutical preparation of urokinase

US4530787A
(en)

1984-03-28
1985-07-23
Cetus Corporation
Controlled oxidation of microbially produced cysteine-containing proteins

US4748234A
(en)

1985-06-26
1988-05-31
Cetus Corporation
Process for recovering refractile bodies containing heterologous proteins from microbial hosts

US4766205A
(en)

1985-11-13
1988-08-23
Beatrice Companies, Inc.
Method for isolation of recombinant polypeptides in biologically active forms

FR2596360B1
(en)

1986-04-01
1989-02-17
Sotralentz Sa

CONTAINER ON PALLET WITH FOLDED AND REINFORCED MESH PROTECTION DEVICE

JPH0651119A
(en)

1992-07-28
1994-02-25
Sekisui Chem Co Ltd
Production of phase difference plate

1985

1985-10-23
DE
DE19853537708
patent/DE3537708A1/en
active
Granted

1986

1986-10-10
IE
IE268386A
patent/IE62634B1/en
not_active
IP Right Cessation

1986-10-15
IL
IL80325A
patent/IL80325A/en
not_active
IP Right Cessation

1986-10-17
CZ
CS867526A
patent/CZ280727B6/en
not_active
IP Right Cessation

1986-10-17
SK
SK7526-86A
patent/SK278317B6/en
unknown

1986-10-21
SI
SI8611796A
patent/SI8611796B/en
unknown

1986-10-21
YU
YU179686A
patent/YU47185B/en
unknown

1986-10-22
DD
DD29546886A
patent/DD260517A5/en
not_active
IP Right Cessation

1986-10-22
CA
CA000521121A
patent/CA1329157C/en
not_active
Expired – Lifetime

1986-10-22
ZA
ZA868012A
patent/ZA868012B/en
unknown

1986-10-23
AT
AT90109721T
patent/ATE131489T1/en
not_active
IP Right Cessation

1986-10-23
AT
AT86114731T
patent/ATE98648T1/en
not_active
IP Right Cessation

1986-10-23
DE
DE3650449T
patent/DE3650449D1/en
not_active
Expired – Lifetime

1986-10-23
EP
EP86906320A
patent/EP0253823A1/en
active
Pending

1986-10-23
ES
ES86114731T
patent/ES2061434T3/en
not_active
Expired – Lifetime

1986-10-23
EP
EP86114731A
patent/EP0219874B1/en
not_active
Expired – Lifetime

1986-10-23
ES
ES90109721T
patent/ES2020498T3/en
not_active
Expired – Lifetime

1986-10-23
PT
PT83609A
patent/PT83609B/en
not_active
IP Right Cessation

1986-10-23
WO
PCT/EP1986/000610
patent/WO1987002673A2/en
active
IP Right Grant

1986-10-23
JP
JP61505882A
patent/JPH0728745B2/en
not_active
Expired – Lifetime

1986-10-23
KR
KR1019870700536A
patent/KR900009139B1/en
not_active
IP Right Cessation

1986-10-23
UA
UA4202987A
patent/UA6023A1/en
unknown

1986-10-23
EP
EP90109721A
patent/EP0393725B1/en
not_active
Expired – Lifetime

1986-10-23
AU
AU65993/86A
patent/AU590029B2/en
not_active
Ceased

1986-10-23
HU
HU865290A
patent/HU204855B/en
unknown

1986-10-23
DE
DE86114731T
patent/DE3689404D1/en
not_active
Expired – Lifetime

1986-10-23
HU
HU865290A
patent/HUT43643A/en
unknown

1987

1987-06-22
FI
FI872753A
patent/FI94050C/en
not_active
IP Right Cessation

1987-06-22
SU
SU874202987Q
patent/SU1607689A3/en
active

1987-06-23
DK
DK198703203A
patent/DK175091B1/en
not_active
IP Right Cessation

1989

1989-09-13
AU
AU41321/89A
patent/AU607083B2/en
not_active
Expired

1991

1991-04-12
JP
JP3079762A
patent/JPH0824594B2/en
not_active
Expired – Lifetime

1992

1992-08-31
GR
GR92300062T
patent/GR920300062T1/en
unknown

1992-10-16
HR
HRP-1796/86A
patent/HRP921075B1/en
not_active
IP Right Cessation

1993

1993-09-03
FI
FI933868A
patent/FI95578C/en
not_active
IP Right Cessation

1995

1995-12-14
GR
GR950403376T
patent/GR3018410T3/en
unknown

1996

1996-08-08
HK
HK153596A
patent/HK153596A/en
not_active
IP Right Cessation

1996-08-08
HK
HK153496A
patent/HK153496A/en
not_active
IP Right Cessation

2000

2000-12-18
DK
DK200001897A
patent/DK175109B1/en
not_active
IP Right Cessation

Cited By (3)

* Cited by examiner, † Cited by third party

Publication number
Priority date
Publication date
Assignee
Title

AU602664B2
(en)

AU609645B2
(en)

1988-10-17
1991-05-02
Boehringer Mannheim Gmbh
Process for the activation of gene-technologically produced, biologically-active proteins expressed in prokaryotes

WO1992004382A1
(en)

1990-09-05
1992-03-19
Bunge (Australia) Pty. Ltd.
Solubilization of proteins in active forms

Also Published As

Publication number
Publication date

IL80325A0
(en)

1987-01-30

WO1987002673A2
(en)

1987-05-07

EP0393725B1
(en)

1995-12-13

CZ280727B6
(en)

1996-04-17

DK200001897A
(en)

2000-12-18

HUT43643A
(en)

1987-11-30

DD260517A5
(en)

1988-09-28

KR900009139B1
(en)

1990-12-22

AU607083B2
(en)

1991-02-21

ES2020498A4
(en)

1991-08-16

ZA868012B
(en)

1987-06-24

KR870700601A
(en)

1987-12-30

EP0253823A1
(en)

1988-01-27

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