CS257789B2 - Method of contaminated peptic or protein products purifying acquired by means of rdna technics - Google Patents
Method of contaminated peptic or protein products purifying acquired by means of rdna technics Download PDFInfo
- Publication number
- CS257789B2 CS257789B2 CS853684A CS368485A CS257789B2 CS 257789 B2 CS257789 B2 CS 257789B2 CS 853684 A CS853684 A CS 853684A CS 368485 A CS368485 A CS 368485A CS 257789 B2 CS257789 B2 CS 257789B2
- Authority
- CS
- Czechoslovakia
- Prior art keywords
- product
- contaminated
- contaminants
- lps
- humulin
- Prior art date
Links
- 238000000034 method Methods 0.000 title claims abstract description 34
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 18
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 18
- 230000001175 peptic effect Effects 0.000 title 1
- 239000000356 contaminant Substances 0.000 claims abstract description 38
- 230000002209 hydrophobic effect Effects 0.000 claims abstract description 20
- 238000000909 electrodialysis Methods 0.000 claims abstract description 15
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 14
- 230000000813 microbial effect Effects 0.000 claims abstract description 9
- 239000002158 endotoxin Substances 0.000 claims description 44
- 229920006008 lipopolysaccharide Polymers 0.000 claims description 39
- 241000588724 Escherichia coli Species 0.000 claims description 19
- 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 claims description 17
- 102000004877 Insulin Human genes 0.000 claims description 8
- 229940125396 insulin Drugs 0.000 claims description 8
- 108090001061 Insulin Proteins 0.000 claims description 7
- 102000002265 Human Growth Hormone Human genes 0.000 claims description 3
- 108010000521 Human Growth Hormone Proteins 0.000 claims description 3
- 239000000854 Human Growth Hormone Substances 0.000 claims description 3
- 102000014150 Interferons Human genes 0.000 claims description 3
- 108010050904 Interferons Proteins 0.000 claims description 3
- 229940079322 interferon Drugs 0.000 claims description 3
- 238000000926 separation method Methods 0.000 claims description 2
- 238000000746 purification Methods 0.000 abstract description 12
- 238000010367 cloning Methods 0.000 abstract 1
- 239000000047 product Substances 0.000 description 40
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 28
- 108010090613 Human Regular Insulin Proteins 0.000 description 23
- 102000013266 Human Regular Insulin Human genes 0.000 description 23
- 229940103471 humulin Drugs 0.000 description 23
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 10
- 238000000502 dialysis Methods 0.000 description 7
- 238000002474 experimental method Methods 0.000 description 7
- 241001646716 Escherichia coli K-12 Species 0.000 description 6
- 238000005227 gel permeation chromatography Methods 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 241000699670 Mus sp. Species 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 210000004408 hybridoma Anatomy 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 239000012264 purified product Substances 0.000 description 3
- 238000012286 ELISA Assay Methods 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 241000239218 Limulus Species 0.000 description 2
- 229920005654 Sephadex Polymers 0.000 description 2
- 239000012507 Sephadex™ Substances 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 108010023197 Streptokinase Proteins 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 230000027455 binding Effects 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- AAOVKJBEBIDNHE-UHFFFAOYSA-N diazepam Chemical compound N=1CC(=O)N(C)C2=CC=C(Cl)C=C2C=1C1=CC=CC=C1 AAOVKJBEBIDNHE-UHFFFAOYSA-N 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 230000008105 immune reaction Effects 0.000 description 2
- 230000016784 immunoglobulin production Effects 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 229910052697 platinum Inorganic materials 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 238000005160 1H NMR spectroscopy Methods 0.000 description 1
- 102100027324 2-hydroxyacyl-CoA lyase 1 Human genes 0.000 description 1
- 101000689231 Aeromonas salmonicida S-layer protein Proteins 0.000 description 1
- 208000002109 Argyria Diseases 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 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 1
- 241000282412 Homo Species 0.000 description 1
- 101001009252 Homo sapiens 2-hydroxyacyl-CoA lyase 1 Proteins 0.000 description 1
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- VVQNEPGJFQJSBK-UHFFFAOYSA-N Methyl methacrylate Chemical compound COC(=O)C(C)=C VVQNEPGJFQJSBK-UHFFFAOYSA-N 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 229920005372 Plexiglas® Polymers 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 101000993800 Sus scrofa Insulin Proteins 0.000 description 1
- 101000748795 Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) Cytochrome c oxidase polypeptide I+III Proteins 0.000 description 1
- RTAQQCXQSZGOHL-UHFFFAOYSA-N Titanium Chemical compound [Ti] RTAQQCXQSZGOHL-UHFFFAOYSA-N 0.000 description 1
- VYWQTJWGWLKBQA-UHFFFAOYSA-N [amino(hydroxy)methylidene]azanium;chloride Chemical compound Cl.NC(N)=O VYWQTJWGWLKBQA-UHFFFAOYSA-N 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 239000002269 analeptic agent Substances 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000001851 biosynthetic effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000004027 cell Anatomy 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 108010072542 endotoxin binding proteins Proteins 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 239000000677 immunologic agent Substances 0.000 description 1
- 229940124541 immunological agent Drugs 0.000 description 1
- 239000003547 immunosorbent Substances 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000012454 limulus amebocyte lysate test Methods 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000000693 micelle Substances 0.000 description 1
- 239000012569 microbial contaminant Substances 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 229910001414 potassium ion Inorganic materials 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000002203 pretreatment Methods 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 230000001698 pyrogenic effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- KKNIUBFRGPFELP-UHFFFAOYSA-N secretolin Chemical compound N=1C=CNC=1CC(N)C(=O)NC(CO)C(=O)NC(CC(O)=O)C(=O)NCC(=O)NC(C(C)O)C(=O)NC(C(=O)NC(C(=O)NC(CO)C(=O)NC(CCC(O)=O)C(=O)NC(CC(C)C)C(=O)NC(CO)C(=O)NC(CCCNC(N)=N)C(=O)NC(CC(C)C)C(=O)NC(CCCNC(N)=N)C(=O)NC(CC(O)=O)C(=O)NC(CO)C(=O)NC(C)C(=O)NC(CCCNC(N)=N)C(=O)NC(CC(C)C)C(=O)NC(CCC(N)=O)C(=O)NC(CCCNC(N)=N)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(CCC(N)=O)C(=O)NCC(=O)NC(CC(C)C)C(=O)NC(C(C)C)C(O)=O)C(C)O)CC1=CC=CC=C1 KKNIUBFRGPFELP-UHFFFAOYSA-N 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 229910052719 titanium Inorganic materials 0.000 description 1
- 239000010936 titanium Substances 0.000 description 1
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
- 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
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D61/00—Processes of separation using semi-permeable membranes, e.g. dialysis, osmosis or ultrafiltration; Apparatus, accessories or auxiliary operations specially adapted therefor
- B01D61/42—Electrodialysis; Electro-osmosis ; Electro-ultrafiltration; Membrane capacitive deionization
- B01D61/44—Ion-selective electrodialysis
-
- 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
- C07K14/575—Hormones
- C07K14/62—Insulins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D2311/00—Details relating to membrane separation process operations and control
- B01D2311/04—Specific process operations in the feed stream; Feed pretreatment
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Urology & Nephrology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Wood Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Hematology (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Immunology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Water Supply & Treatment (AREA)
- General Engineering & Computer Science (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Diabetes (AREA)
- Endocrinology (AREA)
- Gastroenterology & Hepatology (AREA)
- Analytical Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Cell Biology (AREA)
- Food Science & Technology (AREA)
- Toxicology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Plant Pathology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE8402861A SE8402861L (sv) | 1984-05-28 | 1984-05-28 | Rening av biologiskt material |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CS368485A2 CS368485A2 (en) | 1987-11-12 |
| CS257789B2 true CS257789B2 (en) | 1988-06-15 |
Family
ID=20356050
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CS853684A CS257789B2 (en) | 1984-05-28 | 1985-05-22 | Method of contaminated peptic or protein products purifying acquired by means of rdna technics |
Country Status (20)
| Country | Link |
|---|---|
| US (1) | US4746647A (en]) |
| EP (1) | EP0185700A1 (en]) |
| JP (1) | JPS61502378A (en]) |
| KR (1) | KR860700135A (en]) |
| AU (1) | AU4435885A (en]) |
| BR (1) | BR8506758A (en]) |
| CS (1) | CS257789B2 (en]) |
| DD (1) | DD241748A5 (en]) |
| DK (1) | DK39786D0 (en]) |
| ES (3) | ES8609474A1 (en]) |
| FI (1) | FI860316A0 (en]) |
| HU (1) | HUT39774A (en]) |
| IL (1) | IL75258A0 (en]) |
| IN (1) | IN162119B (en]) |
| NO (1) | NO860295L (en]) |
| NZ (1) | NZ212155A (en]) |
| PL (1) | PL253664A1 (en]) |
| SE (1) | SE8402861L (en]) |
| WO (1) | WO1985005631A1 (en]) |
| ZA (1) | ZA853918B (en]) |
Families Citing this family (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1986002068A1 (en) * | 1984-09-26 | 1986-04-10 | Takeda Chemical Industries, Ltd. | Mutual separation of proteins |
| DE3526096A1 (de) * | 1985-07-22 | 1987-01-22 | Basf Ag | Verfahren zur reinigung von htnf |
| US4894439A (en) * | 1986-05-22 | 1990-01-16 | Cetus Corporation | N-terminal derivatives of tumor necrosis factor purified by microporous PTFE membranes |
| US4798886A (en) * | 1986-03-24 | 1989-01-17 | Takeda Chemical Industries, Ltd. | Mutual separation of proteins |
| JPH0789951B2 (ja) * | 1986-06-18 | 1995-10-04 | 財団法人阪大微生物病研究会 | 遺伝子発現産物の精製法 |
| US4940456A (en) * | 1987-02-10 | 1990-07-10 | Dan Sibalis | Electrolytic transdermal delivery of proteins |
| DE3724442A1 (de) * | 1987-07-23 | 1989-02-02 | Europ Lab Molekularbiolog | Verfahren und vorrichtung zur reinigung von m-13-phagen-dna |
| US5147779A (en) * | 1988-06-01 | 1992-09-15 | Miles Inc. | Method for evaluating immunogenicity |
| AUPP521298A0 (en) * | 1998-08-12 | 1998-09-03 | Life Therapeutics Limited | Purification of fibrinogen |
| AUPP790898A0 (en) | 1998-12-23 | 1999-01-28 | Life Therapeutics Limited | Renal dialysis |
| AUPP790698A0 (en) | 1998-12-23 | 1999-01-28 | Life Therapeutics Limited | Separation of microorganisms |
| US20050224355A1 (en) * | 1999-12-23 | 2005-10-13 | Brendon Conlan | Removal of biological contaminants |
| AUPP971399A0 (en) | 1999-04-12 | 1999-05-06 | Life Therapeutics Limited | Separation of plasma components |
| US7077942B1 (en) | 1999-12-23 | 2006-07-18 | Gradipore Limited | Removal of biological contaminants |
| AUPQ691400A0 (en) * | 2000-04-14 | 2000-05-11 | Life Therapeutics Limited | Separation of micromolecules |
| AUPQ697300A0 (en) | 2000-04-18 | 2000-05-11 | Life Therapeutics Limited | Separation apparatus |
| JP2003531362A (ja) | 2000-04-18 | 2003-10-21 | グラディポア・リミテッド | 試料の電気泳動性分離および処理 |
| US6923896B2 (en) * | 2000-09-22 | 2005-08-02 | The Texas A&M University System | Electrophoresis apparatus and method |
| JP2004510170A (ja) * | 2000-10-06 | 2004-04-02 | グラディポア リミテッド | マルチポート型分離装置および方法 |
| AUPR222300A0 (en) * | 2000-12-21 | 2001-01-25 | Life Therapeutics Limited | Electrophoresis device and method |
| US20030232401A1 (en) * | 2002-06-12 | 2003-12-18 | Pugia Michael J. | Bacterial test method by glycated label binding |
| GB201204756D0 (en) * | 2012-03-19 | 2012-05-02 | Lewi Paulus J | Triazines with suitable spacers for treatment and/or prevention of HIV infections |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1188519A (en) * | 1966-10-27 | 1970-04-15 | Wellcome Found | Method for the Purification of Lipopolysaccharides |
| US4185090A (en) * | 1972-02-02 | 1980-01-22 | Abbott Laboratories | Chemically modified endotoxin immunizing agent |
| SE7804098L (sv) * | 1977-04-20 | 1978-10-21 | R & Z Vermoegensverw Gmbh | Peptidkomplex fran dna-haltiga organismer |
| US4321192A (en) * | 1980-01-10 | 1982-03-23 | Ionics Incorporated | Fractionation of protein mixtures by salt addition followed by dialysis treatment |
| US4322275A (en) * | 1980-01-10 | 1982-03-30 | Ionics Incorporated | Fractionation of protein mixtures |
| US4426323A (en) * | 1980-01-10 | 1984-01-17 | Ionics, Incorporated | Selected recovery of proteins from fermentation broths |
| US4351710A (en) * | 1980-01-10 | 1982-09-28 | Ionics, Incorporated | Fractionation of protein mixtures |
| US4276140A (en) * | 1980-01-10 | 1981-06-30 | Ionics Inc. | Electrodialysis apparatus and process for fractionating protein mixtures |
| SE8205892D0 (sv) * | 1982-10-18 | 1982-10-18 | Bror Morein | Immunogent membranproteinkomplex, sett for framstellning och anvendning derav som immunstimulerande medel och sasom vaccin |
| JPS6078999A (ja) * | 1983-10-05 | 1985-05-04 | Chemo Sero Therapeut Res Inst | ＨＢｓ抗原の精製方法 |
| JPS61103895A (ja) * | 1984-10-26 | 1986-05-22 | Green Cross Corp:The | ＨＢｓＡｇの精製方法 |
-
1984
- 1984-05-28 SE SE8402861A patent/SE8402861L/xx not_active Application Discontinuation
-
1985
- 1985-05-21 IL IL75258A patent/IL75258A0/xx unknown
- 1985-05-22 NZ NZ212155A patent/NZ212155A/xx unknown
- 1985-05-22 CS CS853684A patent/CS257789B2/cs unknown
- 1985-05-22 IN IN389/CAL/85A patent/IN162119B/en unknown
- 1985-05-23 ZA ZA853918A patent/ZA853918B/xx unknown
- 1985-05-24 FI FI860316A patent/FI860316A0/fi not_active Application Discontinuation
- 1985-05-24 BR BR8506758A patent/BR8506758A/pt unknown
- 1985-05-24 US US06/834,336 patent/US4746647A/en not_active Expired - Fee Related
- 1985-05-24 AU AU44358/85A patent/AU4435885A/en not_active Abandoned
- 1985-05-24 DD DD85276680A patent/DD241748A5/de not_active IP Right Cessation
- 1985-05-24 WO PCT/SE1985/000218 patent/WO1985005631A1/en not_active Application Discontinuation
- 1985-05-24 EP EP85902715A patent/EP0185700A1/en not_active Withdrawn
- 1985-05-24 JP JP60502612A patent/JPS61502378A/ja active Pending
- 1985-05-24 HU HU853023A patent/HUT39774A/hu unknown
- 1985-05-27 ES ES543512A patent/ES8609474A1/es not_active Expired
- 1985-05-28 PL PL25366485A patent/PL253664A1/xx unknown
-
1986
- 1986-01-27 DK DK39786A patent/DK39786D0/da not_active Application Discontinuation
- 1986-01-28 NO NO860295A patent/NO860295L/no unknown
- 1986-01-28 KR KR860700047A patent/KR860700135A/ko not_active Ceased
- 1986-02-28 ES ES552518A patent/ES8802583A1/es not_active Expired
- 1986-02-28 ES ES552519A patent/ES8802584A1/es not_active Expired
Also Published As
| Publication number | Publication date |
|---|---|
| KR860700135A (ko) | 1986-03-31 |
| PL253664A1 (en) | 1986-02-11 |
| FI860316L (fi) | 1986-01-22 |
| FI860316A7 (fi) | 1986-01-22 |
| WO1985005631A1 (en) | 1985-12-19 |
| DD241748A5 (de) | 1986-12-24 |
| CS368485A2 (en) | 1987-11-12 |
| ES8609474A1 (es) | 1986-08-01 |
| FI860316A0 (fi) | 1986-01-22 |
| SE8402861L (sv) | 1985-11-29 |
| DK39786A (da) | 1986-01-27 |
| ES8802583A1 (es) | 1988-08-01 |
| AU4435885A (en) | 1985-12-31 |
| NO860295L (no) | 1986-01-28 |
| BR8506758A (pt) | 1986-09-23 |
| HUT39774A (en) | 1986-10-29 |
| ES8802584A1 (es) | 1988-08-01 |
| ZA853918B (en) | 1986-01-29 |
| ES543512A0 (es) | 1986-08-01 |
| SE8402861D0 (sv) | 1984-05-28 |
| IL75258A0 (en) | 1985-09-29 |
| EP0185700A1 (en) | 1986-07-02 |
| ES552518A0 (es) | 1988-08-01 |
| IN162119B (en]) | 1988-04-02 |
| ES552519A0 (es) | 1988-08-01 |
| JPS61502378A (ja) | 1986-10-23 |
| NZ212155A (en) | 1988-10-28 |
| DK39786D0 (da) | 1986-01-27 |
| US4746647A (en) | 1988-05-24 |
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