CN1355064A - Composite affinity polyamide film for purifying immone globulin in human blood plasma and preparing process thereof - Google Patents
Composite affinity polyamide film for purifying immone globulin in human blood plasma and preparing process thereof Download PDFInfo
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- CN1355064A CN1355064A CN 00123338 CN00123338A CN1355064A CN 1355064 A CN1355064 A CN 1355064A CN 00123338 CN00123338 CN 00123338 CN 00123338 A CN00123338 A CN 00123338A CN 1355064 A CN1355064 A CN 1355064A
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- phenylalanine
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- 239000004952 Polyamide Substances 0.000 title claims abstract description 16
- 239000002131 composite material Substances 0.000 title claims abstract description 16
- 229920002647 polyamide Polymers 0.000 title claims abstract description 16
- 238000000034 method Methods 0.000 title claims description 13
- 210000002381 plasma Anatomy 0.000 title abstract description 18
- 230000008569 process Effects 0.000 title description 2
- 102000006395 Globulins Human genes 0.000 title 1
- 108010044091 Globulins Proteins 0.000 title 1
- 239000012528 membrane Substances 0.000 claims abstract description 38
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 21
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims abstract description 21
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 21
- 229920000663 Hydroxyethyl cellulose Polymers 0.000 claims abstract description 20
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims abstract description 19
- 239000004354 Hydroxyethyl cellulose Substances 0.000 claims abstract description 18
- 235000019447 hydroxyethyl cellulose Nutrition 0.000 claims abstract description 15
- 239000003446 ligand Substances 0.000 claims abstract description 10
- 238000000746 purification Methods 0.000 claims abstract description 10
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 claims description 11
- CTQNGGLPUBDAKN-UHFFFAOYSA-N O-Xylene Chemical compound CC1=CC=CC=C1C CTQNGGLPUBDAKN-UHFFFAOYSA-N 0.000 claims description 11
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 claims description 10
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 claims description 8
- 238000001035 drying Methods 0.000 claims description 6
- 230000004913 activation Effects 0.000 claims description 5
- 239000008096 xylene Substances 0.000 claims description 5
- 229910000029 sodium carbonate Inorganic materials 0.000 claims description 4
- 238000003756 stirring Methods 0.000 claims description 4
- LZKGFGLOQNSMBS-UHFFFAOYSA-N 4,5,6-trichlorotriazine Chemical compound ClC1=NN=NC(Cl)=C1Cl LZKGFGLOQNSMBS-UHFFFAOYSA-N 0.000 claims 3
- 239000012982 microporous membrane Substances 0.000 claims 2
- 150000001408 amides Chemical class 0.000 claims 1
- 108010074605 gamma-Globulins Proteins 0.000 abstract description 13
- 238000011084 recovery Methods 0.000 abstract description 7
- 230000000694 effects Effects 0.000 abstract description 2
- 239000011148 porous material Substances 0.000 abstract 1
- 239000000243 solution Substances 0.000 description 21
- 238000006243 chemical reaction Methods 0.000 description 11
- RTNUTCOTGVKVBR-UHFFFAOYSA-N 4-chlorotriazine Chemical class ClC1=CC=NN=N1 RTNUTCOTGVKVBR-UHFFFAOYSA-N 0.000 description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- 239000008367 deionised water Substances 0.000 description 9
- 229910021641 deionized water Inorganic materials 0.000 description 9
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 9
- PXFBZOLANLWPMH-UHFFFAOYSA-N 16-Epiaffinine Natural products C1C(C2=CC=CC=C2N2)=C2C(=O)CC2C(=CC)CN(C)C1C2CO PXFBZOLANLWPMH-UHFFFAOYSA-N 0.000 description 8
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 7
- 239000004677 Nylon Substances 0.000 description 7
- 229920001778 nylon Polymers 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 150000001875 compounds Chemical class 0.000 description 6
- MGNCLNQXLYJVJD-UHFFFAOYSA-N cyanuric chloride Chemical compound ClC1=NC(Cl)=NC(Cl)=N1 MGNCLNQXLYJVJD-UHFFFAOYSA-N 0.000 description 5
- 230000007062 hydrolysis Effects 0.000 description 4
- 238000006460 hydrolysis reaction Methods 0.000 description 4
- 238000001291 vacuum drying Methods 0.000 description 4
- GAWIXWVDTYZWAW-UHFFFAOYSA-N C[CH]O Chemical group C[CH]O GAWIXWVDTYZWAW-UHFFFAOYSA-N 0.000 description 3
- 229920002292 Nylon 6 Polymers 0.000 description 3
- 229920002678 cellulose Polymers 0.000 description 3
- 239000001913 cellulose Substances 0.000 description 3
- 239000000835 fiber Substances 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 229920000936 Agarose Polymers 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 239000003480 eluent Substances 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 230000003472 neutralizing effect Effects 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 238000000967 suction filtration Methods 0.000 description 2
- WFYCZPSRMLYGSK-UHFFFAOYSA-N 1,4-dioxane;1,2-xylene Chemical compound C1COCCO1.CC1=CC=CC=C1C WFYCZPSRMLYGSK-UHFFFAOYSA-N 0.000 description 1
- 239000004606 Fillers/Extenders Substances 0.000 description 1
- 108091006027 G proteins Proteins 0.000 description 1
- 102000030782 GTP binding Human genes 0.000 description 1
- 108091000058 GTP-Binding Proteins 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000005903 acid hydrolysis reaction Methods 0.000 description 1
- 125000003368 amide group Chemical group 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 229910052801 chlorine Inorganic materials 0.000 description 1
- 125000001309 chloro group Chemical group Cl* 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 102000034238 globular proteins Human genes 0.000 description 1
- 108091005896 globular proteins Proteins 0.000 description 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 238000007654 immersion Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 238000004900 laundering Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- FEMOMIGRRWSMCU-UHFFFAOYSA-N ninhydrin Chemical compound C1=CC=C2C(=O)C(O)(O)C(=O)C2=C1 FEMOMIGRRWSMCU-UHFFFAOYSA-N 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- OQUKIQWCVTZJAF-UHFFFAOYSA-N phenol;sulfuric acid Chemical compound OS(O)(=O)=O.OC1=CC=CC=C1 OQUKIQWCVTZJAF-UHFFFAOYSA-N 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000012207 quantitative assay Methods 0.000 description 1
- 239000004627 regenerated cellulose Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
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- Separation Using Semi-Permeable Membranes (AREA)
- External Artificial Organs (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Abstract
一种用于人血浆中免疫球蛋白纯化的聚酰胺复合亲和膜,其特征在于:该膜为键合有苯丙氨酸亲和配基的由羟乙基纤维素改性的聚酰胺微孔滤膜复合膜;羟乙基纤维素的量为每克膜15－225mg,苯丙氨酸亲和配基的量为每克膜150～180μmol。本发明对血浆中丙种球蛋白的纯化效果好,介质性能稳定,使用方便,回收率高。A polyamide composite affinity membrane used for purification of immunoglobulin in human plasma, characterized in that: the membrane is a polyamide microstructure modified by hydroxyethyl cellulose bonded with a phenylalanine affinity ligand. Pore filter membrane composite membrane; the amount of hydroxyethyl cellulose is 15-225 mg per gram of membrane, and the amount of phenylalanine affinity ligand is 150-180 μmol per gram of membrane. The invention has good purifying effect on gamma globulin in blood plasma, stable medium performance, convenient use and high recovery rate.
Description
The present invention relates to the diffusion barrier technology, a kind of composite affinity polyamide film and preparation method who is used for the human plasma immunoglobulin purification is provided especially.
The present immunoglobulin purification method of bibliographical information, great majority obtain with ethanol precipitation, but it can only get off various immunoglobulin (Ig) coprecipitations, different types of immunoglobulin (Ig) can not be separated, and products obtained therefrom purity is also undesirable.Someone adopts with agarose, regenerated cellulose, nylon membrane is raw material, immobilized A albumen or the G albumen gone up, and the immunoglobulin (Ig) in the adsorbed plasma gets off the immunoglobulin (Ig) desorption that adsorbs on the above-mentioned medium with salt and organic solvent more specifically.Yet this method is very trouble because A albumen and G protein Preparation are got up, and price is also very expensive, also might cause the inactivation and the sex change of immunoglobulin (Ig) in the elution process, also fails the application that puts it over.Somebody a kind of ectogenous agglutinine-Jacalin immobilized on the agarose Sepharose in addition, but also purifying immunoglobulin (Ig), but the purity of gained immunoglobulin (Ig) and the rate of recovery are all not really desirable.
The object of the present invention is to provide a kind of composite affinity polyamide film and preparation method who is used for the human plasma immunoglobulin purification, it has the higher affine capacity of gamma globulin matter, and the gained gamma globulin has higher purity.
The invention provides a kind of composite affinity polyamide film that is used for the human plasma immunoglobulin purification, it is characterized in that: this film be bonding have the phenylalanine affinity ligand by hydroxyethyl cellulose modified polyamide miillpore filter composite membrane; The amount of hydroxyethylcellulose is every gram film 15～225mg, and the amount of phenylalanine affinity ligand is every gram film 150～180 μ mol.
The present invention also provides the above-mentioned preparation method who is used for the composite affinity polyamide film of human plasma immunoglobulin purification, it is characterized in that:
Polyamide miillpore filter (nylon 6 films) is hydrolyzed with concentrated hydrochloric acid;
Get the PA membrane after the 1g hydrolysis, put into the dimethylbenzene system that 50～150ml contains 30～60% dioxane, the three chlorotriazine methods that add 0.5～1g again in this system respectively activate, and reaction was at room temperature carried out 30～60 minutes;
Film after the activation of three chlorotriazines immerses and contains in 1～5% hydroxy ethyl fiber cellulose solution, and adds sodium carbonate, and the pH value of solution value is remained between 6～7, reacts 2～4 hours down in 40～60 ℃;
With compound behind the film drying under reduced pressure of hydroxyethylcellulose, immerse once more in the above-mentioned dioxane/xylene solution that contains three chlorotriazines, add phenylalanine, 40～60 C reaction 4～5 hours.
Difference with the prior art of the present invention is:
1. selecting micropore nylon 6 films first for use is raw material, activate with three chlorotriazine methods, on the covalent bonding hydroxyethylcellulose, but increased the number of reactive group on the film greatly, and reduced non-specific adsorption to protein except that immunoglobulin (Ig);
2. on prepared nylon 6-hydroxyethylcellulose composite membrane, select dioxane-dimethylbenzene system for use first, by with three chlorotriazines on the reaction key of the active chlorine atom phenylalanine affinity ligand that closed, make that the aglucon number has improved the affine capacity of medium greatly up to 150～180 μ mol/g on the film;
3. under selected best affine condition, this affinity membrane can reach 15～25mg/g film to the affine capacity of gamma globulin matter in the human plasma, and is higher by about 50% than common affinity media, and the purity of gained gamma globulin is 80～85%.
In a word, the affinity membrane that the present invention developed has aglucon bonded amount height, purification effect to gamma globulin in the blood plasma is good, dielectric behavior is stable, easy to use, characteristics such as rate of recovery height are effective tool and the means of producing high purity immune globulin, have very strong practicality and application value.
Below by embodiment in detail the present invention is described in detail.
Embodiment 1
At first polyamide miillpore filter (nylon 6 films) is hydrolyzed with concentrated hydrochloric acid, makes the amide groups on the film change primary amino radical as much as possible into, number of amino groups is carried out quantitative assay with improved ninhydrin method on the film of hydrolysis front and back.
PA membrane after the hydrolysis soaks with NaOH solution, and after fully neutralizing remaining HCl, uses D-H
2O fully washs, suction filtration, and carries out vacuum drying, uses three chlorotriazine method (CyCl then
3) activate, add three chlorotriazines of 0.8g by the 1g PA membrane, to carry out in (V/V) dioxane/dimethylbenzene system that is reflected at 1: 1, reaction was at room temperature carried out 60 minutes, after reaction finishes, used dioxane earlier, used a large amount of D-H again
2O fully washs, and the reduced vacuum drying.
Film after the activation of three chlorotriazines immerses and contains in the 3% hydroxy ethyl fiber cellulose solution, and adds an amount of sodium carbonate, and the pH value of solution value is remained between 6～7.Reacted 4 hours down in 60 ℃, wash 3 times with 0.1mol NaOH solution then, use massive laundering again, and decompressing and extracting; Adopt phenol-sulfuric acid method to measure the amount of hydroxyethylcellulose compound on the nylon membrane, by glucose unit on the cellulosic molecule.The film of compound hydroxyethylcellulose increases about 17 times than the group number that can react on the original nylon membrane, and composite membrane has also significantly reduced the non-specific adsorption to large biological molecule except that immunoglobulin (Ig).
With compound behind the film drying under reduced pressure of hydroxyethylcellulose, immerse once more in the above-mentioned dioxane/xylene solution that contains three chlorotriazines, add phenylalanine, reaction is 5 hours under 40～50 ℃ of stirrings, thoroughly wash with dioxane, aqueous isopropanol and deionized water respectively then, and drying under reduced pressure, so just made the nylon 6-hydroxyethylcellulose composite affinity membrane that contains the phenylalanine affinity ligand, the content of phenylalanine can reach 165 μ mol on every gram film.
With 20 diameters of preparation as stated above is the affinity membrane of 47mm band phenylalanine dentate, is assemblied in the dish formula affinity membrane separator.Use 0.05mol/L NaH
2PO
4Solution dilution 4ml human plasma pumps into affinity membrane separator with plasma extender with the flow velocity of 1ml/min, makes that phenylalanine dentate and gamma globulin produce affine interaction on the film.Earlier under the 2ml/min flow velocity, wash away foreign protein residual on the film with 1mol/L sodium chloride solution 50ml, used 1mol/L sodium chloride/ethylene glycol again instead (1: 1, V/V), the immunoglobulin (Ig) of affine absorption on wash-out film under the same flow (γ-Globulin), collect eluent, after the bag filter dialysis, sample is done electrophoretic analysis, prove that gained gamma immune globular protein purity is 83.5%.The rate of recovery of gamma globulin can reach 78% in the blood plasma, than the rate of recovery height of other purification process.
Embodiment 2
PA membrane after embodiment 1 hydrolysis is soaked with NaOH solution, and after fully neutralizing remaining HCl, use D-H
2O fully washs, suction filtration, and carries out vacuum drying, uses three chlorotriazine method (CyCl then
3) activate, add three chlorotriazines of 1g by the 1g PA membrane, carry out in (V/V) dioxane/dimethylbenzene system that is reflected at 1: 1.
Film after the activation of three chlorotriazines immerses and contains in the 5% hydroxy ethyl fiber cellulose solution, and adds an amount of sodium carbonate, and the pH value of solution value is remained between 6～7.The film of compound hydroxyethylcellulose increases about 20 times than the group number that can react on the original nylon membrane.
With compound behind the film drying under reduced pressure of hydroxyethylcellulose, immerse once more in the above-mentioned dioxane/xylene solution that contains three chlorotriazines, add phenylalanine, reaction is 5 hours under 40～50 ℃ of stirrings, thoroughly wash with dioxane, aqueous isopropanol and deionized water respectively then, and drying under reduced pressure, so just made the nylon 6-hydroxyethylcellulose composite affinity membrane that contains the phenylalanine affinity ligand, the content of phenylalanine can reach 175 μ mol on every gram film.
Embodiment 3
1g contains 25mmol/L Na through the PA membrane immersion 20ml of hydrochloric acid hydrolysis
2CO
3(pH8.0) and 1, in the reaction system of 4-butanediol diglycidyl ether (BDE), under 40 ℃-50 ℃, react 8-10h while stirring.Reaction is used isopropyl alcohol/deionized water (D-H of 1: 1 respectively after finishing
2O) and deionized water take out in a large number and wash film, thoroughly to wash unreacted BDE off.And then film immersed contain in the aqueous solution of 2%HEC, with 2mol/L KOH solution pH value is transferred to 11, react 2-3h in 25 ℃-35 ℃ times, use 0.5mol/L NaHCO respectively
3Solution and deionized water are thoroughly taken out and are washed till cleaning solution and are neutral.The PA membrane that combines HEC is inserted the deionized water by 20ml, 4ml BDE and 80mg KBH
4Under 25 ℃-35 ℃, react 2-4h in the reaction solution of forming, use a large amount of deionized water rinsing films then.Again the film of cleaning is inserted 20ml by 0.5mol/L NaHCO
3In the solution of forming with 100mg phenylalanine (Phe) in 60-70 ℃ of reaction 2-4h down, kept at room temperature overnight.With deionized water reacted film is thoroughly cleaned again, and immersed in the 0.2mol/L beta-mercaptoethanol solution (pH7.0), place 4h under the room temperature, frequent during this time agitated-film, with unreacted active group on the closing membrane, thoroughly clean vacuum drying again with deionized water.Affinity ligand (Phe) content of bonding is 205 μ mol/g on this film after measured, a little more than the affinity membrane with the preparation of three chlorotriazine bonding methods.
With 20 prepared affinity membranes diameter of packing into is in the dish formula affinity membrane separator of 47mm, allows 5ml contain 0.05mol/L NaH
2PO
4The human plasma sample of solution pumps in this separator with the flow velocity of 1ml/min, makes aglucon and the gamma globulin in the blood plasma on the film produce affine interaction.Elder generation's 25ml 1mol/L NaCl/ ethylene glycol (1: 1, V/V) affine gamma globulin on wash-out film under the same flow is collected eluent, after dialysis, do purity analysis with electrophoresis, the purity that proves this gamma globulin is 86.4%, the rate of recovery is 82.0%, a little more than three chlorotriazine methods.
Comparative example
The Ago-Gel Sepharose 4B that the foreign literature report adopts Pharmacia company to produce is a host material, and with phenylalanine dentate on the cyanogen bromide activation bonding, the aglucon bonded amount is 78 μ mol/ml, is lower than bonded amount of the present invention.A volume with this affinity media filling is about 20mlSepharose 4B-Phe affinity column, a purifying 5ml plasma sample, and the purity of gained immunoglobulin (Ig) is 80～82%, a little less than the present invention.The rate of recovery of gamma globulin is 75% in the blood plasma.Approach result of the present invention.
Claims (2)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNB001233386A CN1173771C (en) | 2000-11-29 | 2000-11-29 | Polyamide Composite Affinity Membrane for Purification of Immunoglobulin in Human Plasma and Its Preparation |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CNB001233386A CN1173771C (en) | 2000-11-29 | 2000-11-29 | Polyamide Composite Affinity Membrane for Purification of Immunoglobulin in Human Plasma and Its Preparation |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN1355064A true CN1355064A (en) | 2002-06-26 |
| CN1173771C CN1173771C (en) | 2004-11-03 |
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ID=4589789
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CNB001233386A Expired - Fee Related CN1173771C (en) | 2000-11-29 | 2000-11-29 | Polyamide Composite Affinity Membrane for Purification of Immunoglobulin in Human Plasma and Its Preparation |
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Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113692420A (en) * | 2019-04-08 | 2021-11-23 | 旭化成医疗株式会社 | Polyamide medium for purifying protein-containing solutions and method for producing same |
-
2000
- 2000-11-29 CN CNB001233386A patent/CN1173771C/en not_active Expired - Fee Related
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113692420A (en) * | 2019-04-08 | 2021-11-23 | 旭化成医疗株式会社 | Polyamide medium for purifying protein-containing solutions and method for producing same |
| CN113692420B (en) * | 2019-04-08 | 2023-09-12 | 旭化成医疗株式会社 | Polyamide medium for purifying protein-containing solution and method for producing same |
| US12383884B2 (en) | 2019-04-08 | 2025-08-12 | Asahi Kasei Medical Co., Ltd. | Polyamide medium for purifying protein-containing solution and method for producing polyamide medium |
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| Publication number | Publication date |
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| CN1173771C (en) | 2004-11-03 |
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