WO1997003092A1 - Procede pour eliminer le polyethyleneglycol d'une solution de proteines ou de peptides - Google Patents
Procede pour eliminer le polyethyleneglycol d'une solution de proteines ou de peptides Download PDFInfo
- Publication number
- WO1997003092A1 WO1997003092A1 PCT/DK1996/000314 DK9600314W WO9703092A1 WO 1997003092 A1 WO1997003092 A1 WO 1997003092A1 DK 9600314 W DK9600314 W DK 9600314W WO 9703092 A1 WO9703092 A1 WO 9703092A1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- protein
- solution
- peptide
- peg
- process according
- Prior art date
Links
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 76
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 76
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 62
- 238000000034 method Methods 0.000 title claims abstract description 53
- 229920001223 polyethylene glycol Polymers 0.000 title claims description 92
- 239000002202 Polyethylene glycol Substances 0.000 title claims description 5
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims abstract description 118
- -1 Polyethylene Polymers 0.000 claims abstract description 6
- 239000000243 solution Substances 0.000 claims description 74
- 238000001914 filtration Methods 0.000 claims description 18
- 102000009027 Albumins Human genes 0.000 claims description 7
- 108010088751 Albumins Proteins 0.000 claims description 7
- 102000004506 Blood Proteins Human genes 0.000 claims description 7
- 108010017384 Blood Proteins Proteins 0.000 claims description 7
- 238000005406 washing Methods 0.000 claims description 7
- 108050005077 Haptoglobin Proteins 0.000 claims description 3
- 102000014702 Haptoglobin Human genes 0.000 claims description 3
- 108060003951 Immunoglobulin Proteins 0.000 claims description 3
- 239000007864 aqueous solution Substances 0.000 claims description 3
- 102000018358 immunoglobulin Human genes 0.000 claims description 3
- 229940072221 immunoglobulins Drugs 0.000 claims description 3
- 230000001376 precipitating effect Effects 0.000 claims description 3
- 239000012460 protein solution Substances 0.000 claims description 3
- 102000015081 Blood Coagulation Factors Human genes 0.000 claims description 2
- 108010039209 Blood Coagulation Factors Proteins 0.000 claims description 2
- 241001465754 Metazoa Species 0.000 claims description 2
- 101800004937 Protein C Proteins 0.000 claims description 2
- 102000017975 Protein C Human genes 0.000 claims description 2
- 102000029301 Protein S Human genes 0.000 claims description 2
- 108010066124 Protein S Proteins 0.000 claims description 2
- 229940096437 Protein S Drugs 0.000 claims description 2
- 101800001700 Saposin-D Proteins 0.000 claims description 2
- 102000004338 Transferrin Human genes 0.000 claims description 2
- 108090000901 Transferrin Proteins 0.000 claims description 2
- 239000003114 blood coagulation factor Substances 0.000 claims description 2
- 229920002678 cellulose Polymers 0.000 claims description 2
- 239000001913 cellulose Substances 0.000 claims description 2
- 230000000295 complement effect Effects 0.000 claims description 2
- 229960000856 protein c Drugs 0.000 claims description 2
- 238000003756 stirring Methods 0.000 claims description 2
- 239000012581 transferrin Substances 0.000 claims description 2
- 239000002753 trypsin inhibitor Substances 0.000 claims description 2
- 102000004411 Antithrombin III Human genes 0.000 claims 1
- 108090000935 Antithrombin III Proteins 0.000 claims 1
- 229960005348 antithrombin iii Drugs 0.000 claims 1
- 229910052799 carbon Inorganic materials 0.000 claims 1
- 238000009629 microbiological culture Methods 0.000 claims 1
- 238000004161 plant tissue culture Methods 0.000 claims 1
- 238000005194 fractionation Methods 0.000 abstract description 7
- 238000001179 sorption measurement Methods 0.000 abstract description 5
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 3
- 230000006920 protein precipitation Effects 0.000 abstract description 2
- 239000004698 Polyethylene Substances 0.000 abstract 1
- 229920000573 polyethylene Polymers 0.000 abstract 1
- 229920002560 Polyethylene Glycol 3000 Polymers 0.000 description 11
- 238000001556 precipitation Methods 0.000 description 8
- 102000008100 Human Serum Albumin Human genes 0.000 description 6
- 108091006905 Human Serum Albumin Proteins 0.000 description 6
- 238000004519 manufacturing process Methods 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- 239000003795 chemical substances by application Substances 0.000 description 5
- 108010074605 gamma-Globulins Proteins 0.000 description 5
- 238000011084 recovery Methods 0.000 description 5
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 4
- 239000008118 PEG 6000 Substances 0.000 description 4
- 229920002584 Polyethylene Glycol 6000 Polymers 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
- 229920001030 Polyethylene Glycol 4000 Polymers 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 210000002381 plasma Anatomy 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 2
- 230000003171 anti-complementary effect Effects 0.000 description 2
- 230000008033 biological extinction Effects 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 229920001577 copolymer Polymers 0.000 description 2
- 238000004042 decolorization Methods 0.000 description 2
- 238000011026 diafiltration Methods 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 239000008241 heterogeneous mixture Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 description 2
- VLTRZXGMWDSKGL-UHFFFAOYSA-N perchloric acid Chemical compound OCl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-N 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 1
- 239000005635 Caprylic acid (CAS 124-07-2) Substances 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 229920002565 Polyethylene Glycol 400 Polymers 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 239000004019 antithrombin Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- WDIHJSXYQDMJHN-UHFFFAOYSA-L barium chloride Chemical compound [Cl-].[Cl-].[Ba+2] WDIHJSXYQDMJHN-UHFFFAOYSA-L 0.000 description 1
- 229910001626 barium chloride Inorganic materials 0.000 description 1
- SGUXGJPBTNFBAD-UHFFFAOYSA-L barium iodide Chemical compound [I-].[I-].[Ba+2] SGUXGJPBTNFBAD-UHFFFAOYSA-L 0.000 description 1
- 229940075444 barium iodide Drugs 0.000 description 1
- 229910001638 barium iodide Inorganic materials 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 230000000951 immunodiffusion Effects 0.000 description 1
- 238000000760 immunoelectrophoresis Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 229960003511 macrogol Drugs 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 229960002446 octanoic acid Drugs 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 238000005191 phase separation Methods 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000011045 prefiltration Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 239000012085 test solution Substances 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
Classifications
-
- 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
- C07K1/34—Extraction; Separation; Purification by filtration, ultrafiltration or reverse osmosis
Definitions
- a process for removal of polyethylene glycol from a protein or peptide solution A process for removal of polyethylene glycol from a protein or peptide solution.
- the present invention relates to a method for the removal of polyethylene glycol (hereinafter designated PEG) from a protein or peptide solution.
- PEG polyethylene glycol
- Hask ⁇ et al. (Haematologia 14 (2), 199-206 (1981)) describes a method for fractionation of plasma proteins with PEG-4000 and examine the effects of pH, ionic strenght and temperature.
- a method of protein fractionation suitable for large scale production is described by Bj ⁇ rling (Vox Sang. 49, 240-243 (1985)).
- the method take advantage of the high protein- binding capacity of ion exchangers under special conditions in the presence of PEG.
- Danish patent application No. 646/84 describes a method for manufacturing of a high purity concentrate of Factor VLU by fractionation with PEG in at least two steps, in which one of the steps is a precipitation with PEG in the presence of a salting-in agent.
- US patent specification No. 4,164,495 describes a method for recovering IgG in a pure and anticomplementary activity free condition by fractionated precipitation of blood plasma with PEG in the presence of caprylic acid.
- European patent application having publication number 123,375 describes manufacturing of a dry ⁇ -globulin preparation capable of intravenous injection by fractionating human plasma with PEG.
- the method provides a ⁇ -globulin preparation with improved water solubility and stability against increase of anticomplementary activity and decrease of antibody titer.
- the protein fractions obtained by the PEG fractionation methods generally contains residual PEG and it may, uierefore, be desirable to remove or reduce the content of PEG, especially if the purified protein is used as a drug in mammals.
- the removal of contaminating PEG from a protein fraction may be carried out according to known methods of protein fractionation such as precipitation of the proteins with another precipitation agent or adsorbtion of the proteins on a chromatography column.
- Precipitation with another precipitation agent ethanol, ammonium sulfate a.o.
- introduces other substances that subsequently has to be removed, and adsorbtion of the proteins to a chromatography column may give rise to high concentrations of elution substances after elution of the proteins from the chromatography material.
- European patent application having publication number 123,375 describes a method for removal of PEG from a solution of ⁇ -globulin by treatment with a nonpolar styrene divinylbenzene copolymer.
- the adsorbtion treatment is carried out, batchwise or by a column method, by contacting an aqueous solution of ⁇ -globulin contaminated with PEG to remove the PEG from the aqueous solution by adsorbtion of PEG to the synthetic copolymer.
- PEG may also be removed by diafiltration, as described in European patent application having publication number 270,025, but some proteins tend to aggregate at the ultrafiltration membrane, building up a secondary and denser membrane, that reduces the permeability of PEG.
- the diafiltration time will, therefore, be very long, especially if the PEG is of a high molecular weight, such as PEG-3000 or PEG-4000.
- PEG can be removed from a protein or peptide solution, which process comprises adsorbtion of PEG to activated carbon.
- This absorbtion can be done by filtration of the protein or peptide solution through a filter containing activated carbon.
- PEG may also be removed by adding activated carbon to the PEG containing protein or peptide solution, and then removing the activated carbon by centrifugation or filtration, or by leading the solution through a column with activated carbon.
- This invention relates to a process for removing PEG from a protein or peptide solution.
- the PEG containing solution may have been obtained by a process by which PEG is used in a provisional purification of the protein or peptide in question.
- PEG is removed from this protein or peptide solution by adsorbing the PEG to activated carbon.
- Polyethylene glycol or poly(ethylene oxide) or polyoxyethylene or simply PEG is a water soluble polymer with the general chemical formula: HOCH 2 CH 2 (CH 2 CH 2 O) n CH 2 CH 2 OH, wherein n is an integer.
- polyethylene glycols have designations containing a figure, which figure is the approximate average molecular weight.
- PEG-3000 or Macrogol 3000 signify heterogeneous mixtures having nominal average molecular weights of 3000.
- PEG 400 and PEG 4000 signify heterogeneous mixtures having nominal average molecular weights of 400 and 4000, respectively.
- PEG is a well-known agent for fractional precipitation which stems primarily from its benign chemical properties. Unlike ethanol and other organic precipitating agents, PEG has little tendency to denature or otherwise interact with proteins even when present at high concentrations and elevated temperamres.
- the process of this invention is performed by contacting the PEG containing protein or peptide solution with activated carbon and, thereafter, removing the activated carbon.
- the removal of the activated carbon is to be performed in such a way that the resulting protein or peptide solution has a substantially lower content of PEG, compared with the content of protein or peptide, than the content of PEG in the parent protein solution.
- the protein or peptide solution from which PEG is to be removed is preferably an aqueuos protein or peptide solution containing PEG.
- Activated carbon or activated charcoal is commercial available as a non-soluble porous powder or granular with grains of different sizes or mesh. Activated carbon is videly used in the chemical and pharmaceutical industry for decolorisation or organic contaminant retention. Activated carbon filters are commercial available as filter sheets, filter pads, or filter cartrigdes in which the finely pulverised activated carbon is bonded to a non-migrating fibre matrix made by e.g. cellulose.
- the protein or peptide to be purified may be any protein or peptide obtained from plants, animals, or microbes including proteins or peptides obtained by recombinant technology.
- the protein is especially a plasma protein selected from the group consisting of albumin, immunoglobulins, coagulation factors, antithrombin HI, protein C, protein S, complement factors, transferrin, haptoglobin, ⁇ 2 -macroglobulin, and ⁇ ,-antitrypsin.
- the protein is selected from immuglobulins and albumin.
- the activated carbon is added to the PEG-containing protein or peptide solution batchwise, and after stirring for a period of time that is sufficient for adsorbing the PEG, the activated carbon is separated from the solution by methods known per se such as centrifugation, sedimitation, or filtration.
- the removed activated carbon may subsequently be washed and the washing solution may be added to the purified, more protein or peptide containing solution, to increase the recovery of, for example, a valuable protein or peptide in the purified solution.
- granular activated carbon is packed into a column.
- the PEG-containing protein or peptide solution is then led through the column and the effluent is collected.
- the column may subsequently be washed and the washing solution may be added to the purified more protein or peptide containing solution, to increase the recovery of, for example, a valuable protein or peptide in the purified solution.
- the PEG-containing protein or peptide solution is filtered through an activated carbon filter with a flow rate that permits the adsorbtion of the PEG to the activated carbon in the filter.
- the removal of the PEG by filtration may be combined with the removal of other contaminating substances, with a decolorization, or with a clarification of the solution by the activated carbon filter.
- the filtration may be performed by techniques known per se and with known equipments usually obtainable from the manufacturer of the filters.
- the filter may subsequently be washed and the washing solution may be added to the purified more protein or peptide containing solution, to increase the recovery of e.g. a valuable protein or peptide in the treated solution.
- Another aspect of this invention is a process for purifying a PEG containing solution of a protein or peptide, which process comprises precipitating the protein or peptide with PEG, resolubilizing the precipitated protein or peptide and treating the resolubilised protein or peptide solution with activated carbon.
- the desired protein or peptide is extracted from the purified protein or peptide solution in a manner known per se, for example, by lyophilization.
- the PEG content was determined by means of spectrophotometric measurements of the extinction value at 535 nm after formation of a complex of with barium iodide: 1000 ⁇ l of 0.5 M perchloric acid was added to 200 ⁇ l of test solution, in duplo standard solutions (10 - 75 ⁇ g/ml), and blind sample (destilled water) in centrifuge glasses and mixed thoroughly. After at least 15 minutes, the solutions were centrifuged for 15 minutes at 3000 ⁇ m. To 10 800 ⁇ l of the supernatants were added 200 ⁇ l of a 5 % barium chloride solution. For each 30 seconds 100 ⁇ l of iodine-R (0.1 M) was added to all test tubes and mixed thoroughly. After exactly 20 minutes the extinction value at 535 nm were measured towards the blind sample.
- IgG was measured by radial immuno diffusion towards rabbit anti-human IgG (A-424, 15 DAKO, Denmark).
- Amount of activated carbon PEG mg/ml IgG, mg/ml added, g/25 ml
- Example 3 A 20 % solution of human serum albumin (HSA) (ALBUMIN Novo Nordisk, Gentofte, Denmark) was diluted until a concentration of 3% HSA and 2.55 g/litre of PEG-3000 was added. The pH value was adjusted to 5.0. 830 ml of this solution was then filtered through an AKS-4 activated carbon filter from Seitz (Seitz-Filter-Werke, Bad Kreuznach, Germany). The filter area was 143 cm 2 . Samples of 100 ml of the filtered solution was collected and PEG was determined similarly as described in example 1. The data are given in table 3.
- HSA human serum albumin
- the concentration of PEG was determined to 2600 ⁇ g/ml. After filtration of 300 ml of the PEG-containing HSA-solution, more than 90 % of PEG was removed, corresponding to an adsorbtion of about 5 mg PEG/cm 2 of filter-area. No adso ⁇ tion of HSA to the filter was observed.
- PEG was measured similarly as described in example 1 and HSA was measured by rocket immuno electrophoresis towards rabbit anti-Human Albumin (A001 , DAKO, Denmark).
- Example 4 Resolubilized crude-IgG was obtained from the routine production of Nordimmun ® .
- the crude-IgG was obtained by precipitation with PEG-3000, and the precipitate, therefore contained residual amounts of PEG-3000.
- Crude-IgG consist of the human plasma proteins IgG, IgA, IgM, albumin, haptoglobin, and ⁇ 2 -macroglobulin.
- Samples of resolubilized crude-IgG were then filtered through an In line 90 filter housing (filter area 64 cm 2 ) from CUNO equiped with either Zeta plus activated carbon R 33 SLP (CUNO), or Zeta plus activated carbon R 53 SLP (CUNO).
- the filters were of pharmaceutical grade.
- a sample of resolubilized crude-IgG was centrifugated and filtered through one of the filters. 50 ml samples of filtrate were collected and PEG and IgG were determined analogous as described in example 1 (table 4).
- the concentration of PEG and IgG were 3.91 mg/ml and 86.6 mg/ml before filtration, respectively.
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Analytical Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Water Supply & Treatment (AREA)
- Peptides Or Proteins (AREA)
Abstract
Le polyéthylène est utilisé pour la précipitation fractionnaire des protéines et des peptides. Les fractions de protéines et de peptides obtenues selon les méthodes de fractionnement par PEG contiennent généralement des résidus de PEG. La présente invention concerne un procédé permettant d'éliminer d'une solution de protéines ou de peptides le PEG contaminant, lequel procédé consiste à adsorber le PEG contenu dans la solution sur un carbone activé.
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK0823/95 | 1995-07-13 | ||
| DK82395 | 1995-07-13 | ||
| DK0970/95 | 1995-09-04 | ||
| DK97095 | 1995-09-04 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO1997003092A1 true WO1997003092A1 (fr) | 1997-01-30 |
Family
ID=26064723
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/DK1996/000314 WO1997003092A1 (fr) | 1995-07-13 | 1996-07-10 | Procede pour eliminer le polyethyleneglycol d'une solution de proteines ou de peptides |
Country Status (1)
| Country | Link |
|---|---|
| WO (1) | WO1997003092A1 (fr) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2012062998A1 (fr) | 2010-11-08 | 2012-05-18 | Institut National Polytechnique De Lorraine | Procede de purification d'un melange visqueux contenant un ou plusieurs contaminants |
| WO2017045617A1 (fr) * | 2015-09-17 | 2017-03-23 | 中国人民解放军军事医学科学院野战输血研究所 | Procédé de séparation et de purification d'α2-macroglobuline à partir d'un sédiment de constituant iv de cohn |
| US9910041B2 (en) | 2013-07-12 | 2018-03-06 | Emd Millipore Corporation | Method of determining virus removal from a sample containing a target protein using activated carbon |
| EP3643722A1 (fr) * | 2012-08-07 | 2020-04-29 | Kyowa Kirin Co., Ltd. | Procédé de purification de protéine |
| US11472836B2 (en) * | 2013-02-26 | 2022-10-18 | Emd Millipore Corporation | Selective removal of a protein from a mixture of proteins using activated carbon by adjusting solution conditions |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3966702A (en) * | 1973-07-16 | 1976-06-29 | Ralston Purina Company | Process for the production of oilseed isolates |
| US4164495A (en) * | 1976-04-06 | 1979-08-14 | Nordisk Insulinlaboratorium | Method of recovering immunoglobulin using a polyol and an alkanoic acid |
| US4404285A (en) * | 1981-06-24 | 1983-09-13 | Amf Incorporated | Process for preparing a zero standard serum |
-
1996
- 1996-07-10 WO PCT/DK1996/000314 patent/WO1997003092A1/fr active Application Filing
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3966702A (en) * | 1973-07-16 | 1976-06-29 | Ralston Purina Company | Process for the production of oilseed isolates |
| US4164495A (en) * | 1976-04-06 | 1979-08-14 | Nordisk Insulinlaboratorium | Method of recovering immunoglobulin using a polyol and an alkanoic acid |
| US4404285A (en) * | 1981-06-24 | 1983-09-13 | Amf Incorporated | Process for preparing a zero standard serum |
Non-Patent Citations (5)
| Title |
|---|
| ANALYTICAL BIOCHEMISTRY, Volume 163, 1987, LIONEL MARCUS et al., "Effect of Particle Size of Activated Charcoal on Separation of Triton X-100 from Protein, Liver Cytosol and Lipoxygenase Extracts", pages 112-116. * |
| CUNO Microfiltration Products, GM 20.1 E, issued 20.07.87, pages 3-4. * |
| DIALOG INFORMATION SERVICES, File 5, Biosis, Dialog Accession No. 6494608, Biosis Accession No. 85095129, OGINO K. et al., "Removal of Humic Substance Dissolved in Water I"; & J. COLLOID INTERFACE SCI. 121 (1), 1988, 161-169. * |
| VOX SANG, Volume 23, 1972, A. POLSON et al., "Fractionation of Plasma with Polyethylene Glycol", pages 107-118. * |
| ZHURNAL MIKROBIOLOGII EPIDEMIOLOGII I IMMUNOBIOLOGII, Volume 4, 1984, IGUDIN L.I. et al., "Polyethylene Glycols and Their Use in Biology and Medicine", pages 17-21. * |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2012062998A1 (fr) | 2010-11-08 | 2012-05-18 | Institut National Polytechnique De Lorraine | Procede de purification d'un melange visqueux contenant un ou plusieurs contaminants |
| EP3643722A1 (fr) * | 2012-08-07 | 2020-04-29 | Kyowa Kirin Co., Ltd. | Procédé de purification de protéine |
| US11472836B2 (en) * | 2013-02-26 | 2022-10-18 | Emd Millipore Corporation | Selective removal of a protein from a mixture of proteins using activated carbon by adjusting solution conditions |
| US9910041B2 (en) | 2013-07-12 | 2018-03-06 | Emd Millipore Corporation | Method of determining virus removal from a sample containing a target protein using activated carbon |
| WO2017045617A1 (fr) * | 2015-09-17 | 2017-03-23 | 中国人民解放军军事医学科学院野战输血研究所 | Procédé de séparation et de purification d'α2-macroglobuline à partir d'un sédiment de constituant iv de cohn |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5808011A (en) | Method for chromatographic removal of prions | |
| JP3094167B2 (ja) | 免疫血清グロブリンの精製方法 | |
| US4216205A (en) | Process of preparing a serum protein composition for intravenous application | |
| SK281839B6 (sk) | Spôsob separácie vopred vybraného druhu hemoglobínu | |
| EP2272870A1 (fr) | Procédé pour la préparation d'immunoglobulines pour l'administration intravéneuse et d'autres produits immunoglobuliniques | |
| JP2008500959A (ja) | ウイルスについて安全な免疫グロブリンの製造方法 | |
| AU2017302006B2 (en) | Process for preparing immunoglobulin compositions | |
| SK287633B6 (sk) | Spôsob výroby humánneho gamaglobulínu G a humánny gamaglobulín G s inaktivovanými vírusmi | |
| US20240092828A1 (en) | Systems and methods for process scale isolation of a protein | |
| US11739117B2 (en) | Therapeutic protein compositions and methods | |
| US20250188119A1 (en) | Method for removing fxi when purifying plasma proteins | |
| WO1997003092A1 (fr) | Procede pour eliminer le polyethyleneglycol d'une solution de proteines ou de peptides | |
| JPS601136A (ja) | 血液製剤中の不適合反応原因物質不活化法 | |
| US12037360B2 (en) | Compositions and methods for isolating proteins | |
| AU731770B2 (en) | Process for removing unconventional transmissible agents from a protein solution | |
| WO2025085544A1 (fr) | Procédé intégré pour isoler des protéines plasmatiques | |
| US20040198957A1 (en) | Method for removing endotoxins from protein solutions | |
| JPH0723319B2 (ja) | 血液製剤から血液型抗体を除去する方法 | |
| HK1151044B (en) | Process for manufacturing immunoglobulins for intravenous administration and other immunoglobulin-like products |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| AK | Designated states |
Kind code of ref document: A1 Designated state(s): JP US |
|
| AL | Designated countries for regional patents |
Kind code of ref document: A1 Designated state(s): AT BE CH DE DK ES FI FR GB GR IE IT LU MC NL PT SE |
|
| DFPE | Request for preliminary examination filed prior to expiration of 19th month from priority date (pct application filed before 20040101) | ||
| 121 | Ep: the epo has been informed by wipo that ep was designated in this application | ||
| WWE | Wipo information: entry into national phase |
Ref document number: 1996922786 Country of ref document: EP |
|
| WWW | Wipo information: withdrawn in national office |
Ref document number: 1996922786 Country of ref document: EP |
|
| 122 | Ep: pct application non-entry in european phase | ||
| 122 | Ep: pct application non-entry in european phase |