NO830697L - Homogent menneske-immun-interferon og fremstilling derav - Google Patents

Homogent menneske-immun-interferon og fremstilling derav

Info

Publication number: NO830697L
Authority: NO; Norway
Prior art keywords: interferon; column; human; immune; active fractions
Prior art date: 1982-03-01

Application number

NO830697A

Other languages

English (en)

Norwegian (no)

Inventor

Stanley Stein

Richard A Wolfe

Original Assignee

Hoffmann La Roche

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.)

1982-03-01

Filing date

1983-02-28

Publication date

1983-09-02

1983-02-28 Application filed by Hoffmann La Roche filed Critical Hoffmann La Roche

1983-09-02 Publication of NO830697L publication Critical patent/NO830697L/no

Links

102000014150 Interferons Human genes 0.000 title claims description 32
108010050904 Interferons Proteins 0.000 title claims description 32
229940079322 interferon Drugs 0.000 title claims description 27
238000004519 manufacturing process Methods 0.000 title claims description 3
101000599940 Homo sapiens Interferon gamma Proteins 0.000 claims description 36
238000000034 method Methods 0.000 claims description 30
230000001965 increasing effect Effects 0.000 claims description 12
239000000243 solution Substances 0.000 claims description 11
238000002360 preparation method Methods 0.000 claims description 10
108010062580 Concanavalin A Proteins 0.000 claims description 9
150000003839 salts Chemical class 0.000 claims description 9
239000000741 silica gel Substances 0.000 claims description 9
229910002027 silica gel Inorganic materials 0.000 claims description 9
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 8
238000004811 liquid chromatography Methods 0.000 claims description 6
238000012784 weak cation exchange Methods 0.000 claims description 6
-1 carboxymethyl silica gel Chemical compound 0.000 claims description 5
239000000463 material Substances 0.000 claims description 5
239000000203 mixture Substances 0.000 claims description 5
239000008057 potassium phosphate buffer Substances 0.000 claims description 5
238000005406 washing Methods 0.000 claims description 4
229920002684 Sepharose Polymers 0.000 claims description 3
239000002552 dosage form Substances 0.000 claims description 2
230000008569 process Effects 0.000 claims description 2
230000003028 elevating effect Effects 0.000 claims 4
239000008366 buffered solution Substances 0.000 claims 2
244000228957 Ferula foetida Species 0.000 claims 1
239000007864 aqueous solution Substances 0.000 claims 1
239000000084 colloidal system Substances 0.000 claims 1
150000002500 ions Chemical class 0.000 claims 1
239000000546 pharmaceutical excipient Substances 0.000 claims 1
108010074328 Interferon-gamma Proteins 0.000 description 15
102000008070 Interferon-gamma Human genes 0.000 description 15
WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 14
210000004027 cell Anatomy 0.000 description 14
108090000623 proteins and genes Proteins 0.000 description 14
102000004169 proteins and genes Human genes 0.000 description 13
108010047620 Phytohemagglutinins Proteins 0.000 description 10
230000000694 effects Effects 0.000 description 10
230000001885 phytohemagglutinin Effects 0.000 description 10
LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 10
238000000746 purification Methods 0.000 description 8
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
LYCAIKOWRPUZTN-UHFFFAOYSA-N ethylene glycol Substances OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 7
239000002609 medium Substances 0.000 description 7
239000001103 potassium chloride Substances 0.000 description 7
235000011164 potassium chloride Nutrition 0.000 description 7
239000000872 buffer Substances 0.000 description 6
230000006698 induction Effects 0.000 description 6
229940047124 interferons Drugs 0.000 description 6
210000000265 leukocyte Anatomy 0.000 description 6
238000005259 measurement Methods 0.000 description 6
150000001413 amino acids Chemical class 0.000 description 5
238000004458 analytical method Methods 0.000 description 5
238000011534 incubation Methods 0.000 description 5
229910000160 potassium phosphate Inorganic materials 0.000 description 5
235000011009 potassium phosphates Nutrition 0.000 description 5
239000006228 supernatant Substances 0.000 description 5
102000006992 Interferon-alpha Human genes 0.000 description 4
108010047761 Interferon-alpha Proteins 0.000 description 4
230000000840 anti-viral effect Effects 0.000 description 4
239000000427 antigen Substances 0.000 description 4
102000036639 antigens Human genes 0.000 description 4
108091007433 antigens Proteins 0.000 description 4
239000003226 mitogen Substances 0.000 description 4
241000283690 Bos taurus Species 0.000 description 3
108091003079 Bovine Serum Albumin Proteins 0.000 description 3
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 3
210000001744 T-lymphocyte Anatomy 0.000 description 3
239000002253 acid Substances 0.000 description 3
238000001042 affinity chromatography Methods 0.000 description 3
229910000318 alkali metal phosphate Inorganic materials 0.000 description 3
238000003556 assay Methods 0.000 description 3
230000004071 biological effect Effects 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
238000004587 chromatography analysis Methods 0.000 description 3
239000012894 fetal calf serum Substances 0.000 description 3
239000001963 growth medium Substances 0.000 description 3
239000000411 inducer Substances 0.000 description 3
PHEDXBVPIONUQT-RGYGYFBISA-N phorbol 13-acetate 12-myristate Chemical compound C([C@]1(O)C(=O)C(C)=C[C@H]1[C@@]1(O)[C@H](C)[C@H]2OC(=O)CCCCCCCCCCCCC)C(CO)=C[C@H]1[C@H]1[C@]2(OC(C)=O)C1(C)C PHEDXBVPIONUQT-RGYGYFBISA-N 0.000 description 3
239000002644 phorbol ester Substances 0.000 description 3
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
239000010452 phosphate Substances 0.000 description 3
239000007858 starting material Substances 0.000 description 3
JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 2
241000282412 Homo Species 0.000 description 2
108090001090 Lectins Proteins 0.000 description 2
102000004856 Lectins Human genes 0.000 description 2
108010033737 Pokeweed Mitogens Proteins 0.000 description 2
QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 2
241000711975 Vesicular stomatitis virus Species 0.000 description 2
229910001508 alkali metal halide Inorganic materials 0.000 description 2
150000008045 alkali metal halides Chemical class 0.000 description 2
229910052936 alkali metal sulfate Inorganic materials 0.000 description 2
210000004369 blood Anatomy 0.000 description 2
239000008280 blood Substances 0.000 description 2
239000007975 buffered saline Substances 0.000 description 2
230000010261 cell growth Effects 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
239000003636 conditioned culture medium Substances 0.000 description 2
XVOYSCVBGLVSOL-UHFFFAOYSA-N cysteic acid Chemical compound OC(=O)C(N)CS(O)(=O)=O XVOYSCVBGLVSOL-UHFFFAOYSA-N 0.000 description 2
230000000120 cytopathologic effect Effects 0.000 description 2
231100000655 enterotoxin Toxicity 0.000 description 2
230000000977 initiatory effect Effects 0.000 description 2
239000002523 lectin Substances 0.000 description 2
238000011068 loading method Methods 0.000 description 2
210000004698 lymphocyte Anatomy 0.000 description 2
244000005700 microbiome Species 0.000 description 2
239000002773 nucleotide Substances 0.000 description 2
125000003729 nucleotide group Chemical group 0.000 description 2
239000008363 phosphate buffer Substances 0.000 description 2
239000011148 porous material Substances 0.000 description 2
239000000047 product Substances 0.000 description 2
239000012266 salt solution Substances 0.000 description 2
239000000377 silicon dioxide Substances 0.000 description 2
241000894007 species Species 0.000 description 2
230000001225 therapeutic effect Effects 0.000 description 2
238000002560 therapeutic procedure Methods 0.000 description 2
CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 2
MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
208000002109 Argyria Diseases 0.000 description 1
235000008733 Citrus aurantifolia Nutrition 0.000 description 1
239000012591 Dulbecco’s Phosphate Buffered Saline Substances 0.000 description 1
210000000712 G cell Anatomy 0.000 description 1
229920001612 Hydroxyethyl starch Polymers 0.000 description 1
102000003996 Interferon-beta Human genes 0.000 description 1
108090000467 Interferon-beta Proteins 0.000 description 1
AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
241000272168 Laridae Species 0.000 description 1
229920002274 Nalgene Polymers 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
241000276498 Pollachius virens Species 0.000 description 1
101150107341 RERE gene Proteins 0.000 description 1
239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
239000004473 Threonine Substances 0.000 description 1
235000011941 Tilia x europaea Nutrition 0.000 description 1
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
YJQCOFNZVFGCAF-UHFFFAOYSA-N Tunicamycin II Natural products O1C(CC(O)C2C(C(O)C(O2)N2C(NC(=O)C=C2)=O)O)C(O)C(O)C(NC(=O)C=CCCCCCCCCC(C)C)C1OC1OC(CO)C(O)C(O)C1NC(C)=O YJQCOFNZVFGCAF-UHFFFAOYSA-N 0.000 description 1
208000036142 Viral infection Diseases 0.000 description 1
241000700605 Viruses Species 0.000 description 1
239000002250 absorbent Substances 0.000 description 1
230000002745 absorbent Effects 0.000 description 1
238000010521 absorption reaction Methods 0.000 description 1
230000009471 action Effects 0.000 description 1
239000002269 analeptic agent Substances 0.000 description 1
230000001028 anti-proliverative effect Effects 0.000 description 1
230000000259 anti-tumor effect Effects 0.000 description 1
239000012062 aqueous buffer Substances 0.000 description 1
239000011324 bead Substances 0.000 description 1
210000000601 blood cell Anatomy 0.000 description 1
239000007853 buffer solution Substances 0.000 description 1
239000006143 cell culture medium Substances 0.000 description 1
230000004663 cell proliferation Effects 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
238000006243 chemical reaction Methods 0.000 description 1
238000010367 cloning Methods 0.000 description 1
239000013065 commercial product Substances 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
239000000470 constituent Substances 0.000 description 1
239000005289 controlled pore glass Substances 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
238000002842 cytophatogenic effect reduction assay Methods 0.000 description 1
230000004665 defense response Effects 0.000 description 1
239000008367 deionised water Substances 0.000 description 1
229910021641 deionized water Inorganic materials 0.000 description 1
238000004925 denaturation Methods 0.000 description 1
230000036425 denaturation Effects 0.000 description 1
238000001514 detection method Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
239000003480 eluent Substances 0.000 description 1
238000011067 equilibration Methods 0.000 description 1
239000012847 fine chemical Substances 0.000 description 1
ZFKJVJIDPQDDFY-UHFFFAOYSA-N fluorescamine Chemical compound C12=CC=CC=C2C(=O)OC1(C1=O)OC=C1C1=CC=CC=C1 ZFKJVJIDPQDDFY-UHFFFAOYSA-N 0.000 description 1
GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
238000009472 formulation Methods 0.000 description 1
238000001502 gel electrophoresis Methods 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
239000011521 glass Substances 0.000 description 1
230000012010 growth Effects 0.000 description 1
230000007062 hydrolysis Effects 0.000 description 1
238000006460 hydrolysis reaction Methods 0.000 description 1
229940050526 hydroxyethylstarch Drugs 0.000 description 1
230000016784 immunoglobulin production Effects 0.000 description 1
230000001506 immunosuppresive effect Effects 0.000 description 1
239000012535 impurity Substances 0.000 description 1
239000004615 ingredient Substances 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
238000002347 injection Methods 0.000 description 1
239000007924 injection Substances 0.000 description 1
238000010255 intramuscular injection Methods 0.000 description 1
239000007927 intramuscular injection Substances 0.000 description 1
238000001990 intravenous administration Methods 0.000 description 1
238000011031 large-scale manufacturing process Methods 0.000 description 1
239000004571 lime Substances 0.000 description 1
230000000873 masking effect Effects 0.000 description 1
HOVAGTYPODGVJG-VEIUFWFVSA-N methyl alpha-D-mannoside Chemical compound CO[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]1O HOVAGTYPODGVJG-VEIUFWFVSA-N 0.000 description 1
230000005012 migration Effects 0.000 description 1
238000013508 migration Methods 0.000 description 1
VIKNJXKGJWUCNN-XGXHKTLJSA-N norethisterone Chemical compound O=C1CC[C@@H]2[C@H]3CC[C@](C)([C@](CC4)(O)C#C)[C@@H]4[C@@H]3CCC2=C1 VIKNJXKGJWUCNN-XGXHKTLJSA-N 0.000 description 1
239000006201 parenteral dosage form Substances 0.000 description 1
230000002093 peripheral effect Effects 0.000 description 1
150000004633 phorbol derivatives Chemical class 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
239000005373 porous glass Substances 0.000 description 1
239000002994 raw material Substances 0.000 description 1
238000011160 research Methods 0.000 description 1
239000011347 resin Substances 0.000 description 1
229920005989 resin Polymers 0.000 description 1
238000004062 sedimentation Methods 0.000 description 1
238000000926 separation method Methods 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
239000011780 sodium chloride Substances 0.000 description 1
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
239000008227 sterile water for injection Substances 0.000 description 1
238000005728 strengthening Methods 0.000 description 1
239000000126 substance Substances 0.000 description 1
230000002195 synergetic effect Effects 0.000 description 1
229960000814 tetanus toxoid Drugs 0.000 description 1
ZHSGGJXRNHWHRS-VIDYELAYSA-N tunicamycin Chemical compound O([C@H]1[C@@H]([C@H]([C@@H](O)[C@@H](CC(O)[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C(NC(=O)C=C2)=O)O)O1)O)NC(=O)/C=C/CC(C)C)[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1NC(C)=O ZHSGGJXRNHWHRS-VIDYELAYSA-N 0.000 description 1
MEYZYGMYMLNUHJ-UHFFFAOYSA-N tunicamycin Natural products CC(C)CCCCCCCCCC=CC(=O)NC1C(O)C(O)C(CC(O)C2OC(C(O)C2O)N3C=CC(=O)NC3=O)OC1OC4OC(CO)C(O)C(O)C4NC(=O)C MEYZYGMYMLNUHJ-UHFFFAOYSA-N 0.000 description 1
229960005486 vaccine Drugs 0.000 description 1
230000009385 viral infection Effects 0.000 description 1

Classifications

- 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]
- C07K14/57—IFN-gamma
- 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]
- 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
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/18—Ion-exchange chromatography
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Medicinal Chemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Biochemistry (AREA)
Molecular Biology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Gastroenterology & Hepatology (AREA)
Toxicology (AREA)
Zoology (AREA)
Analytical Chemistry (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)

NO830697A 1982-03-01 1983-02-28 Homogent menneske-immun-interferon og fremstilling derav NO830697L (no)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US35344282A	1982-03-01	1982-03-01

Publications (1)

Publication Number	Publication Date
NO830697L true NO830697L (no)	1983-09-02

Family

ID=23389118

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO830697A NO830697L (no)	1982-03-01	1983-02-28	Homogent menneske-immun-interferon og fremstilling derav

Country Status (19)

Country	Link
EP (1)	EP0087686A3 (fr)
JP (1)	JPS58159417A (fr)
KR (1)	KR840003422A (fr)
AU (1)	AU1181283A (fr)
DK (1)	DK104283A (fr)
ES (1)	ES8407499A1 (fr)
FI (1)	FI830557L (fr)
GB (1)	GB2119383A (fr)
GR (1)	GR77910B (fr)
GT (1)	GT198301619A (fr)
IL (1)	IL67978A0 (fr)
MC (1)	MC1499A1 (fr)
MT (1)	MTP924B (fr)
MW (1)	MW783A1 (fr)
NO (1)	NO830697L (fr)
NZ (1)	NZ203364A (fr)
PT (1)	PT76310B (fr)
ZA (1)	ZA83768B (fr)
ZW (1)	ZW4683A1 (fr)

Families Citing this family (15)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP0107498B1 (fr) *	1982-10-25	1990-05-16	Genentech, Inc.	Activité synergétique d'interféron humain
IL67896A (en) *	1983-02-13	1987-03-31	Yeda Res & Dev	Two biologically active human gama interferon subtypes,purification thereof and pharmaceutical compositions containing them
DE3484374D1 (de) *	1983-08-04	1991-05-08	Green Cross Corp	Gamma-interferonzusammensetzung.
US4681930A (en) *	1983-09-20	1987-07-21	Hoffmann-La Roche Inc.	Immune interferon and a method for its extraction and purification
MX9203641A (es) *	1983-12-16	1992-07-01	Genentech Inc	Interferones gamma recombinantes que poseen estabilidad mejorada y metodos biotecnologicos para su obtencion.
US4855238A (en) *	1983-12-16	1989-08-08	Genentech, Inc.	Recombinant gamma interferons having enhanced stability and methods therefor
US4946674A (en) *	1984-10-05	1990-08-07	Bioferon Biochemische Substanzen Gmbh & Co.	Process for treatment of rheumatic diseases
IL76591A0 (en) *	1984-10-05	1986-02-28	Bioferon Biochem Substanz	Pharmaceutical compositions containing ifn-ypsilon and processes for the preparation thereof
MA20647A1 (fr) *	1985-03-25	1986-10-01	Schering Corp	Compositions stables a base d'interferon-gamma
GB8508340D0 (en) *	1985-03-29	1985-05-09	Creighton T E	Production of protein
GB8522336D0 (en) *	1985-09-09	1985-10-16	Biogen Nv	Composition for treatment of allergies
WO1987005518A1 (fr) *	1986-03-17	1987-09-24	Schering Corporation	Traitement de cancers a l'aide de l'interferon gamma
IL84170A0 (en) *	1986-10-17	1988-03-31	Interferon Sciences Inc	Method for detecting interferon
EP0276120B1 (fr) *	1987-01-20	1992-04-08	Schering Corporation	Traitement de certaines leucémies avec une association d'interféron gamma et d'interféron alpha
DE102007050165B4 (de) *	2007-10-19	2010-06-17	Stiftung Tierärztliche Hochschule Hannover	Stabilisierte Lösung, Verfahren zu deren Herstellung sowie deren Verwendung und Arzneimittel in Form einer stabilisierten Lösung

Family Cites Families (8)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA120527A (fr) *	1907-05-18	1909-09-14	James Mccallum Robertson	Dispositif a paiement d'avance sur compteurs
CA120526A (fr) *	1909-05-05	1909-09-14	Robert A. Reynolds	Machine a combustion interieure
CA130300A (fr) *	1910-08-03	1911-01-03	John W. Ziegler	Roue pour courant
CA154712A (fr) *	1914-01-02	1914-03-31	William Francis Fox	Procede photographique
CA179241A (fr) *	1917-03-02	1917-09-11	John Totterdale	Bidon
US4241174A (en) *	1978-11-24	1980-12-23	Hoffmann-La Roche Inc.	Interferon assay
IN150740B (fr) *	1978-11-24	1982-12-04	Hoffmann La Roche
CH648331A5 (de) *	1979-07-31	1985-03-15	Hoffmann La Roche	Homogenes fibroblasten-interferon und dessen herstellung.

1983
- 1983-02-04 ZA ZA83768A patent/ZA83768B/xx unknown
- 1983-02-17 EP EP83101522A patent/EP0087686A3/fr not_active Withdrawn
- 1983-02-18 FI FI830557A patent/FI830557L/fi not_active Application Discontinuation
- 1983-02-18 MT MT924A patent/MTP924B/xx unknown
- 1983-02-21 MW MW7/83A patent/MW783A1/xx unknown
- 1983-02-21 ZW ZW46/83A patent/ZW4683A1/xx unknown
- 1983-02-22 NZ NZ203364A patent/NZ203364A/en unknown
- 1983-02-23 IL IL67978A patent/IL67978A0/xx unknown
- 1983-02-24 AU AU11812/83A patent/AU1181283A/en not_active Abandoned
- 1983-02-25 MC MC831624A patent/MC1499A1/fr unknown
- 1983-02-28 GR GR70628A patent/GR77910B/el unknown
- 1983-02-28 JP JP58031081A patent/JPS58159417A/ja active Pending
- 1983-02-28 KR KR1019830000822A patent/KR840003422A/ko not_active Application Discontinuation
- 1983-02-28 GB GB08305506A patent/GB2119383A/en not_active Withdrawn
- 1983-02-28 DK DK104283A patent/DK104283A/da not_active Application Discontinuation
- 1983-02-28 GT GT198301619A patent/GT198301619A/es unknown
- 1983-02-28 PT PT76310A patent/PT76310B/pt unknown
- 1983-02-28 ES ES520164A patent/ES8407499A1/es not_active Expired
- 1983-02-28 NO NO830697A patent/NO830697L/no unknown

Also Published As

Publication number	Publication date
FI830557A0 (fi)	1983-02-18
DK104283A (da)	1983-09-02
IL67978A0 (en)	1983-06-15
DK104283D0 (da)	1983-02-28
JPS58159417A (ja)	1983-09-21
FI830557L (fi)	1983-09-02
GR77910B (fr)	1984-09-25
GT198301619A (es)	1984-08-21
KR840003422A (ko)	1984-09-08
AU1181283A (en)	1983-09-08
ES520164A0 (es)	1984-10-01
GB2119383A (en)	1983-11-16
NZ203364A (en)	1986-07-11
MW783A1 (en)	1984-09-12
GB8305506D0 (en)	1983-03-30
ZW4683A1 (en)	1983-10-19
ZA83768B (en)	1983-10-26
MC1499A1 (fr)	1983-11-17
MTP924B (en)	1984-05-03
EP0087686A3 (fr)	1985-09-18
EP0087686A2 (fr)	1983-09-07
PT76310B (en)	1986-02-12
ES8407499A1 (es)	1984-10-01
PT76310A (en)	1983-03-01

Publication	Publication Date	Title
Yip et al.	1981	Partial purification and characterization of human gamma (immune) interferon.
EP0567554B1 (fr)	1995-04-12	Procede de purification du facteur de croissance-1 analogue a l'insuline, sous une forme intacte et correctement pliee
US6471500B1 (en)	2002-10-29	Process for producing erythropoietin containing no animal proteins
NO830697L (no)	1983-09-02	Homogent menneske-immun-interferon og fremstilling derav
Lai et al.	1976	Chemistry of cholera toxin: the subunit structure
Peumans et al.	1982	Isolation and partial characterization of wheat-germ-agglutinin-like lectins from rye (Secale cereale) and barley (Hordeum vulgare) embryos
EP0110302A2 (fr)	1984-06-13	Procédé de préparation d'interférons monomères
Tsuda	1979	Purification and characterization of a lectin from rice bran
US5196323A (en)	1993-03-23	Process for preparing and purifying alpha-interferon
US5593667A (en)	1997-01-14	Recombinant immune interferon having an intact carboxyl terminus
CA1231306A (fr)	1988-01-12	Epuration de l'interferon
Carra	1965	Purification and N-terminal analyses of algal biliproteins
NO159610B (no)	1988-10-10	Fremgangsm te ved rensing av et immuninterferonfrag
US4765903A (en)	1988-08-23	Purification of monomeric interferon
US4534906A (en)	1985-08-13	Removal of impurities from human leukocyte interferon preparations
GB2055384A (en)	1981-03-04	Homogeneous fibroblast interferon and method for manufacture thereof
US4908432A (en)	1990-03-13	Novel polypeptide having gamma-interferon activity
US4617378A (en)	1986-10-14	Purification of biologically active human immune interferon
CA1340281C (fr)	1998-12-22	Methode pour preparer et purifier des alpha-interferons
JPS6261040B2 (fr)	1987-12-18
Garattini et al.	1986	Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme
Kenny et al.	1981	[64] Purification of human fibroblast interferon produced in the absence of serum by cibacron blue F3GA-agarose and high-performance liquid chromatography
EP0396555B1 (fr)	1992-07-29	Purification d'interferon monomere
MIYATA et al.	1986	Pruification of Natural Human Interferon-Gamma by Antibody Affinity Chromatography: Analysis of Constituent Protein Species in the Dimers
Friesen et al.	1981	[63] Purification of human fibroblast interferon by high-performance liquid chromatography