IL87349A - Water-soluble factor that activates glial cells, its preparation and pharmaceutical compositions comprising it - Google Patents

Water-soluble factor that activates glial cells, its preparation and pharmaceutical compositions comprising it

Info

Publication number: IL87349A
Authority: IL; Israel
Prior art keywords: laminin; cells; peak; fraction; production
Prior art date: 1988-08-04

Application number

IL8734988A

Other languages

English (en)

Other versions

IL87349A0 (en

Inventor

Michal Schwartz

Avi Cohen

Michael Belkin

Original Assignee

Michal Schwartz

Avi Cohen

Michael Belkin

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.)

1988-08-04

Filing date

1988-08-04

Publication date

1994-06-24

1988-08-04 Application filed by Michal Schwartz, Avi Cohen, Michael Belkin filed Critical Michal Schwartz

1988-08-04 Priority to IL8734988A priority Critical patent/IL87349A/en

1989-08-02 Priority to AU39212/89A priority patent/AU628832B2/en

1989-08-03 Priority to HU893952A priority patent/HU209131B/hu

1989-08-03 Priority to FI893685A priority patent/FI93925C/fi

1989-08-04 Priority to ZA895967A priority patent/ZA895967B/xx

1989-08-04 Priority to NZ230207A priority patent/NZ230207A/en

1989-08-04 Priority to PT91379A priority patent/PT91379B/pt

1989-08-04 Priority to EP19890114485 priority patent/EP0353780A3/en

1989-08-04 Priority to KR1019890011156A priority patent/KR900002782A/ko

1989-08-04 Priority to JP1202699A priority patent/JPH0288600A/ja

1989-08-04 Priority to DK384789A priority patent/DK384789A/da

1989-08-04 Priority to MYPI89001059A priority patent/MY131020A/en

1991-03-10 Publication of IL87349A0 publication Critical patent/IL87349A0/xx

1994-06-24 Publication of IL87349A publication Critical patent/IL87349A/en

Links

210000004498 neuroglial cell Anatomy 0.000 title claims description 12
239000008194 pharmaceutical composition Substances 0.000 title claims description 5
238000002360 preparation method Methods 0.000 title description 2
239000003636 conditioned culture medium Substances 0.000 claims description 36
102000004169 proteins and genes Human genes 0.000 claims description 22
108090000623 proteins and genes Proteins 0.000 claims description 22
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 20
210000005036 nerve Anatomy 0.000 claims description 14
210000003169 central nervous system Anatomy 0.000 claims description 13
210000001328 optic nerve Anatomy 0.000 claims description 13
239000007983 Tris buffer Substances 0.000 claims description 12
230000001172 regenerating effect Effects 0.000 claims description 12
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 claims description 12
230000000694 effects Effects 0.000 claims description 11
241000251468 Actinopterygii Species 0.000 claims description 10
239000011780 sodium chloride Substances 0.000 claims description 10
230000004071 biological effect Effects 0.000 claims description 9
238000004519 manufacturing process Methods 0.000 claims description 9
208000032612 Glial tumor Diseases 0.000 claims description 8
206010018338 Glioma Diseases 0.000 claims description 8
238000000034 method Methods 0.000 claims description 8
230000008929 regeneration Effects 0.000 claims description 6
238000011069 regeneration method Methods 0.000 claims description 6
241000124008 Mammalia Species 0.000 claims description 5
238000005349 anion exchange Methods 0.000 claims description 5
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 5
108050001049 Extracellular proteins Proteins 0.000 claims description 4
238000004113 cell culture Methods 0.000 claims description 4
238000004587 chromatography analysis Methods 0.000 claims description 4
238000007873 sieving Methods 0.000 claims description 4
208000027418 Wounds and injury Diseases 0.000 claims description 3
230000006378 damage Effects 0.000 claims description 3
230000001939 inductive effect Effects 0.000 claims description 3
208000014674 injury Diseases 0.000 claims description 3
230000036755 cellular response Effects 0.000 claims description 2
238000010828 elution Methods 0.000 claims description 2
238000002523 gelfiltration Methods 0.000 claims description 2
239000008363 phosphate buffer Substances 0.000 claims description 2
230000015572 biosynthetic process Effects 0.000 claims 1
230000001747 exhibiting effect Effects 0.000 claims 1
238000010438 heat treatment Methods 0.000 claims 1
238000003786 synthesis reaction Methods 0.000 claims 1
210000004027 cell Anatomy 0.000 description 52
102000007547 Laminin Human genes 0.000 description 42
108010085895 Laminin Proteins 0.000 description 42
150000003839 salts Chemical class 0.000 description 12
210000004556 brain Anatomy 0.000 description 7
239000000284 extract Substances 0.000 description 7
238000001114 immunoprecipitation Methods 0.000 description 7
238000002372 labelling Methods 0.000 description 7
239000000203 mixture Substances 0.000 description 7
239000002609 medium Substances 0.000 description 5
239000000126 substance Substances 0.000 description 5
102000016359 Fibronectins Human genes 0.000 description 4
108010067306 Fibronectins Proteins 0.000 description 4
241000283973 Oryctolagus cuniculus Species 0.000 description 4
210000001130 astrocyte Anatomy 0.000 description 4
238000005119 centrifugation Methods 0.000 description 4
238000009826 distribution Methods 0.000 description 4
238000000746 purification Methods 0.000 description 4
238000002965 ELISA Methods 0.000 description 3
208000009331 Experimental Sarcoma Diseases 0.000 description 3
102000010834 Extracellular Matrix Proteins Human genes 0.000 description 3
108010037362 Extracellular Matrix Proteins Proteins 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
241000191967 Staphylococcus aureus Species 0.000 description 3
230000004913 activation Effects 0.000 description 3
210000002744 extracellular matrix Anatomy 0.000 description 3
238000005194 fractionation Methods 0.000 description 3
238000001727 in vivo Methods 0.000 description 3
238000011534 incubation Methods 0.000 description 3
229920001184 polypeptide Polymers 0.000 description 3
108090000765 processed proteins & peptides Proteins 0.000 description 3
102000004196 processed proteins & peptides Human genes 0.000 description 3
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
241000283707 Capra Species 0.000 description 2
239000006144 Dulbecco’s modiﬁed Eagle's medium Substances 0.000 description 2
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
238000009825 accumulation Methods 0.000 description 2
230000003213 activating effect Effects 0.000 description 2
239000004480 active ingredient Substances 0.000 description 2
239000000872 buffer Substances 0.000 description 2
230000001143 conditioned effect Effects 0.000 description 2
238000010166 immunofluorescence Methods 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
210000001428 peripheral nervous system Anatomy 0.000 description 2
YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 2
230000004044 response Effects 0.000 description 2
210000004116 schwann cell Anatomy 0.000 description 2
238000000926 separation method Methods 0.000 description 2
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
239000000243 solution Substances 0.000 description 2
238000012360 testing method Methods 0.000 description 2
FFEARJCKVFRZRR-ZLINWBGDSA-N (2S)-2-amino-4-methyl(33S)sulfanylbutanoic acid Chemical compound N[C@@H](CC[33S]C)C(=O)O FFEARJCKVFRZRR-ZLINWBGDSA-N 0.000 description 1
PCDWFBFHIIKIPM-UHFFFAOYSA-N 3-ethyl-2h-1,3-benzothiazole-2-sulfonic acid Chemical compound C1=CC=C2N(CC)C(S(O)(=O)=O)SC2=C1 PCDWFBFHIIKIPM-UHFFFAOYSA-N 0.000 description 1
HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
241000252229 Carassius auratus Species 0.000 description 1
108060003393 Granulin Proteins 0.000 description 1
108010001336 Horseradish Peroxidase Proteins 0.000 description 1
108090001061 Insulin Proteins 0.000 description 1
102000004877 Insulin Human genes 0.000 description 1
GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 1
206010039491 Sarcoma Diseases 0.000 description 1
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
229920004890 Triton X-100 Polymers 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
239000013543 active substance Substances 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
238000003556 assay Methods 0.000 description 1
230000003376 axonal effect Effects 0.000 description 1
OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
PXXJHWLDUBFPOL-UHFFFAOYSA-N benzamidine Chemical compound NC(=N)C1=CC=CC=C1 PXXJHWLDUBFPOL-UHFFFAOYSA-N 0.000 description 1
229940098773 bovine serum albumin Drugs 0.000 description 1
210000004958 brain cell Anatomy 0.000 description 1
230000004663 cell proliferation Effects 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
230000021617 central nervous system development Effects 0.000 description 1
238000006243 chemical reaction Methods 0.000 description 1
238000012790 confirmation Methods 0.000 description 1
230000002596 correlated effect Effects 0.000 description 1
230000000875 corresponding effect Effects 0.000 description 1
239000000287 crude extract Substances 0.000 description 1
230000007812 deficiency Effects 0.000 description 1
230000003412 degenerative effect Effects 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
239000003599 detergent Substances 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
238000013401 experimental design Methods 0.000 description 1
238000000605 extraction Methods 0.000 description 1
239000011536 extraction buffer Substances 0.000 description 1
239000012894 fetal calf serum Substances 0.000 description 1
239000000706 filtrate Substances 0.000 description 1
MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
238000001502 gel electrophoresis Methods 0.000 description 1
239000011521 glass Substances 0.000 description 1
230000002518 glial effect Effects 0.000 description 1
239000012133 immunoprecipitate Substances 0.000 description 1
238000011065 in-situ storage Methods 0.000 description 1
230000006698 induction Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
238000005342 ion exchange Methods 0.000 description 1
238000002955 isolation Methods 0.000 description 1
GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 1
108010052968 leupeptin Proteins 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
239000000463 material Substances 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
238000013508 migration Methods 0.000 description 1
230000005012 migration Effects 0.000 description 1
230000000877 morphologic effect Effects 0.000 description 1
210000000653 nervous system Anatomy 0.000 description 1
230000001537 neural effect Effects 0.000 description 1
210000002569 neuron Anatomy 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
239000008188 pellet Substances 0.000 description 1
229950000964 pepstatin Drugs 0.000 description 1
108010091212 pepstatin Proteins 0.000 description 1
FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 1
210000000578 peripheral nerve Anatomy 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
238000001243 protein synthesis Methods 0.000 description 1
210000001525 retina Anatomy 0.000 description 1
239000012723 sample buffer Substances 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
239000007858 starting material Substances 0.000 description 1
239000000758 substrate Substances 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
230000014616 translation Effects 0.000 description 1
239000002023 wood Substances 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
- 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
- C07K14/475—Growth factors; Growth regulators
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Medicinal Chemistry (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
Biophysics (AREA)
Genetics & Genomics (AREA)
Gastroenterology & Hepatology (AREA)
Zoology (AREA)
Molecular Biology (AREA)
Toxicology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Chemical Kinetics & Catalysis (AREA)
Neurosurgery (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Pharmacology & Pharmacy (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
General Chemical & Material Sciences (AREA)
Animal Behavior & Ethology (AREA)
Neurology (AREA)
Biomedical Technology (AREA)
Bioinformatics & Cheminformatics (AREA)
Engineering & Computer Science (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Compounds Of Unknown Constitution (AREA)

IL8734988A 1988-08-04 1988-08-04 Water-soluble factor that activates glial cells, its preparation and pharmaceutical compositions comprising it IL87349A (en)

Priority Applications (12)

Application Number	Priority Date	Filing Date	Title
IL8734988A IL87349A (en)	1988-08-04	1988-08-04	Water-soluble factor that activates glial cells, its preparation and pharmaceutical compositions comprising it
AU39212/89A AU628832B2 (en)	1988-08-04	1989-08-02	Activation of target cells
HU893952A HU209131B (en)	1988-08-04	1989-08-03	Process for activating target cells
FI893685A FI93925C (fi)	1988-08-04	1989-08-03	Menetelmä kalan uudistuvista näköhermoista peräisin olevan vesiliukoisen tekijän valmistamiseksi
ZA895967A ZA895967B (en)	1988-08-04	1989-08-04	Activation of target cells
NZ230207A NZ230207A (en)	1988-08-04	1989-08-04	Water soluble factor extracted from fish optical nerve
PT91379A PT91379B (pt)	1988-08-04	1989-08-04	Processo de separacao e purificacao de factor derivado de nervo optico dos peixes e de composicoes farmaceuticas
EP19890114485 EP0353780A3 (en)	1988-08-04	1989-08-04	Factor for the activation of target cells
KR1019890011156A KR900002782A (ko)	1988-08-04	1989-08-04	표적상 적혈구(target cell)의 활성화
JP1202699A JPH0288600A (ja)	1988-08-04	1989-08-04	ラミニン放出因子
DK384789A DK384789A (da)	1988-08-04	1989-08-04	Fremgangsmaade til aktivering af maalceller
MYPI89001059A MY131020A (en)	1988-08-04	1989-08-04	Activation of target cells

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
IL8734988A IL87349A (en)	1988-08-04	1988-08-04	Water-soluble factor that activates glial cells, its preparation and pharmaceutical compositions comprising it

Publications (2)

Publication Number	Publication Date
IL87349A0 IL87349A0 (en)	1991-03-10
IL87349A true IL87349A (en)	1994-06-24

Family

ID=11059128

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
IL8734988A IL87349A (en)	1988-08-04	1988-08-04	Water-soluble factor that activates glial cells, its preparation and pharmaceutical compositions comprising it

Country Status (12)

Country	Link
EP (1)	EP0353780A3 (da)
JP (1)	JPH0288600A (da)
KR (1)	KR900002782A (da)
AU (1)	AU628832B2 (da)
DK (1)	DK384789A (da)
FI (1)	FI93925C (da)
HU (1)	HU209131B (da)
IL (1)	IL87349A (da)
MY (1)	MY131020A (da)
NZ (1)	NZ230207A (da)
PT (1)	PT91379B (da)
ZA (1)	ZA895967B (da)

Families Citing this family (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
IL91459A0 (en) *	1989-08-28	1990-04-29	Yeda Res & Dev	Oligodendrocyte inhibitory factor
IE911318A1 (en) *	1990-04-23	1991-10-23	Yeda Res & Dev	Use of a tumor necrosis factor for facilitating nerve¹regeneration
US5898066A (en) *	1994-08-26	1999-04-27	Children's Medical Center Corporation	Trophic factors for central nervous system regeneration

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
IL71440A0 (en) *	1984-04-04	1984-07-31	Univ Ramot	Composition for nerve regeneration

1988
- 1988-08-04 IL IL8734988A patent/IL87349A/en not_active IP Right Cessation
1989
- 1989-08-02 AU AU39212/89A patent/AU628832B2/en not_active Ceased
- 1989-08-03 HU HU893952A patent/HU209131B/hu not_active IP Right Cessation
- 1989-08-03 FI FI893685A patent/FI93925C/fi not_active IP Right Cessation
- 1989-08-04 NZ NZ230207A patent/NZ230207A/en unknown
- 1989-08-04 JP JP1202699A patent/JPH0288600A/ja active Pending
- 1989-08-04 DK DK384789A patent/DK384789A/da not_active Application Discontinuation
- 1989-08-04 MY MYPI89001059A patent/MY131020A/en unknown
- 1989-08-04 PT PT91379A patent/PT91379B/pt active IP Right Grant
- 1989-08-04 ZA ZA895967A patent/ZA895967B/xx unknown
- 1989-08-04 EP EP19890114485 patent/EP0353780A3/en not_active Withdrawn
- 1989-08-04 KR KR1019890011156A patent/KR900002782A/ko not_active Ceased

Also Published As

Publication number	Publication date
HU209131B (en)	1994-03-28
JPH0288600A (ja)	1990-03-28
ZA895967B (en)	1991-01-30
EP0353780A3 (en)	1991-09-04
IL87349A0 (en)	1991-03-10
AU3921289A (en)	1990-02-08
PT91379A (pt)	1990-03-08
FI93925B (fi)	1995-03-15
DK384789D0 (da)	1989-08-04
HUT52116A (en)	1990-06-28
KR900002782A (ko)	1990-03-23
MY131020A (en)	2007-07-31
FI93925C (fi)	1995-06-26
DK384789A (da)	1990-02-05
FI893685L (fi)	1990-02-05
FI893685A0 (fi)	1989-08-03
PT91379B (pt)	1995-05-04
EP0353780A2 (en)	1990-02-07
NZ230207A (en)	1992-04-28
AU628832B2 (en)	1992-09-24

Legal Events

Date	Code	Title	Description
1999-08-17	RH	Patent void
2003-05-29	MM9K	Patent not in force due to non-payment of renewal fees

Publication	Publication Date	Title
McKerracher et al.	1994	Identification of myelin-associated glycoprotein as a major myelin-derived inhibitor of neurite growth
Asch et al.	1986	Human brain glial cells synthesize thrombospondin.
Ricard-Blum et al.	1982	Biochemical properties and immunolocalization of minor collagens in foetal calf cartilage
Herndon et al.	1973	Immuno-electron microscopic localization of the encephalitogenic basic protein in myelin
US6022540A (en)	2000-02-08	Ligands that modulate differentiation of mesenchymal stem cells
Walker	1982	Isolation from cholinergic synapses of a protein that binds to membranes in a calcium‐dependent manner
Striessnig et al.	1986	Stereoselective photoaffinity labelling of the purified 1, 4‐dihydropyridine receptor of the voltage‐dependent calcium channel
Domenicucci et al.	1988	Characterization of porcine osteonectin extracted from foetal calvariae
Adam et al.	1983	Altered expression of collagen phenotype in osteoarthrosis
JPH075481B2 (ja)	1995-01-25	創傷の治癒
GR1001011B (el)	1993-03-31	Θεραπευτικος παραγων.
Calof et al.	1985	Response of purified chick motoneurons to myotube conditioned medium: laminin is essential for the substratum-binding, neurite outgrowth-promoting activity
Paul et al.	1980	Human platelet basic protein associated with antiheparin and mitogenic activities: purification and partial characterization.
CA2253246A1 (en)	1997-11-06	Purified multimerase
Zimmermann et al.	1973	Intermolecular Cross‐Links of Collagen: Participation of the Carboxy‐Terminal Nonhelical Region of the α1‐Chain
IL87349A (en)	1994-06-24	Water-soluble factor that activates glial cells, its preparation and pharmaceutical compositions comprising it
Dupuy et al.	1989	Thrombin mitogenic responses and protein phosphorylation are different in cultured human endothelial cells derived from large and microvessels
Akahane et al.	1977	Soluble Proteins from Fowl Feather Keratin: I. Fractionation and Properties
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