CA2800155A1 - Method for preparing an enriched igg composition from plasma - Google Patents
Method for preparing an enriched igg composition from plasma Download PDFInfo
- Publication number
- CA2800155A1 CA2800155A1 CA2800155A CA2800155A CA2800155A1 CA 2800155 A1 CA2800155 A1 CA 2800155A1 CA 2800155 A CA2800155 A CA 2800155A CA 2800155 A CA2800155 A CA 2800155A CA 2800155 A1 CA2800155 A1 CA 2800155A1
- Authority
- CA
- Canada
- Prior art keywords
- igg
- precipitate
- solution
- composition
- fraction
- Prior art date
- Legal status (The legal status 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 status listed.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims abstract description 262
- 239000000203 mixture Substances 0.000 title claims abstract description 205
- 239000008194 pharmaceutical composition Substances 0.000 claims abstract description 40
- 238000000746 purification Methods 0.000 claims abstract description 24
- 238000001990 intravenous administration Methods 0.000 claims abstract description 18
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 388
- 239000000243 solution Substances 0.000 claims description 208
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 188
- 238000001556 precipitation Methods 0.000 claims description 180
- 239000002244 precipitate Substances 0.000 claims description 137
- 239000000725 suspension Substances 0.000 claims description 128
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 125
- 108090000623 proteins and genes Proteins 0.000 claims description 110
- 102000004169 proteins and genes Human genes 0.000 claims description 109
- 239000000706 filtrate Substances 0.000 claims description 93
- 239000000872 buffer Substances 0.000 claims description 84
- 238000001914 filtration Methods 0.000 claims description 74
- 229960000583 acetic acid Drugs 0.000 claims description 73
- 238000005507 spraying Methods 0.000 claims description 60
- 239000006228 supernatant Substances 0.000 claims description 59
- 108010049003 Fibrinogen Proteins 0.000 claims description 49
- 102000008946 Fibrinogen Human genes 0.000 claims description 49
- 229940012952 fibrinogen Drugs 0.000 claims description 49
- 230000001376 precipitating effect Effects 0.000 claims description 48
- 239000003599 detergent Substances 0.000 claims description 41
- 238000000108 ultra-filtration Methods 0.000 claims description 41
- 239000007788 liquid Substances 0.000 claims description 38
- 230000000694 effects Effects 0.000 claims description 34
- 239000012362 glacial acetic acid Substances 0.000 claims description 31
- 239000007921 spray Substances 0.000 claims description 30
- 239000012528 membrane Substances 0.000 claims description 27
- 238000011026 diafiltration Methods 0.000 claims description 20
- 239000002904 solvent Substances 0.000 claims description 20
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 claims description 18
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 18
- 238000005119 centrifugation Methods 0.000 claims description 16
- 238000004255 ion exchange chromatography Methods 0.000 claims description 15
- 229910019142 PO4 Inorganic materials 0.000 claims description 14
- 238000002156 mixing Methods 0.000 claims description 14
- 239000000377 silicon dioxide Substances 0.000 claims description 14
- 239000010452 phosphate Substances 0.000 claims description 13
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 13
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 claims description 13
- 229920000053 polysorbate 80 Polymers 0.000 claims description 13
- 235000012239 silicon dioxide Nutrition 0.000 claims description 13
- 208000023275 Autoimmune disease Diseases 0.000 claims description 12
- 238000005571 anion exchange chromatography Methods 0.000 claims description 12
- 238000005277 cation exchange chromatography Methods 0.000 claims description 11
- 208000015181 infectious disease Diseases 0.000 claims description 11
- 238000001728 nano-filtration Methods 0.000 claims description 11
- 238000005406 washing Methods 0.000 claims description 11
- 239000004471 Glycine Substances 0.000 claims description 10
- 230000001154 acute effect Effects 0.000 claims description 10
- 239000011148 porous material Substances 0.000 claims description 10
- 239000012538 diafiltration buffer Substances 0.000 claims description 9
- 239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 claims description 7
- 229940068968 polysorbate 80 Drugs 0.000 claims description 7
- 239000005909 Kieselgur Substances 0.000 claims description 6
- 239000007864 aqueous solution Substances 0.000 claims description 6
- 206010061598 Immunodeficiency Diseases 0.000 claims description 5
- 208000029462 Immunodeficiency disease Diseases 0.000 claims description 5
- 230000007813 immunodeficiency Effects 0.000 claims description 5
- 239000013612 plasmid Substances 0.000 claims description 4
- 238000006243 chemical reaction Methods 0.000 claims description 3
- 238000001816 cooling Methods 0.000 claims 2
- 229920002113 octoxynol Polymers 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 abstract description 48
- 230000002829 reductive effect Effects 0.000 abstract description 32
- 201000010099 disease Diseases 0.000 abstract description 17
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 17
- 238000007920 subcutaneous administration Methods 0.000 abstract description 10
- 238000007918 intramuscular administration Methods 0.000 abstract description 9
- 229940027941 immunoglobulin g Drugs 0.000 description 385
- 235000019441 ethanol Nutrition 0.000 description 214
- 235000018102 proteins Nutrition 0.000 description 100
- 230000006872 improvement Effects 0.000 description 98
- 238000011282 treatment Methods 0.000 description 69
- 238000000605 extraction Methods 0.000 description 68
- 229910002012 Aerosil® Inorganic materials 0.000 description 50
- 238000011534 incubation Methods 0.000 description 42
- 238000005194 fractionation Methods 0.000 description 39
- 238000004090 dissolution Methods 0.000 description 37
- 230000008569 process Effects 0.000 description 37
- 238000002360 preparation method Methods 0.000 description 36
- 230000003024 amidolytic effect Effects 0.000 description 35
- 108060003951 Immunoglobulin Proteins 0.000 description 28
- 102000018358 immunoglobulin Human genes 0.000 description 28
- 238000005352 clarification Methods 0.000 description 27
- 239000011536 extraction buffer Substances 0.000 description 26
- 238000009472 formulation Methods 0.000 description 25
- 238000011084 recovery Methods 0.000 description 25
- 239000012535 impurity Substances 0.000 description 24
- 238000010979 pH adjustment Methods 0.000 description 23
- 239000000047 product Substances 0.000 description 23
- 239000003795 chemical substances by application Substances 0.000 description 20
- 239000012065 filter cake Substances 0.000 description 20
- 229910021485 fumed silica Inorganic materials 0.000 description 19
- 229940099472 immunoglobulin a Drugs 0.000 description 19
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 18
- -1 carboxylate anions Chemical class 0.000 description 16
- 238000002474 experimental method Methods 0.000 description 16
- 238000002560 therapeutic procedure Methods 0.000 description 14
- 239000012141 concentrate Substances 0.000 description 12
- 239000000356 contaminant Substances 0.000 description 12
- 235000021317 phosphate Nutrition 0.000 description 12
- 239000007858 starting material Substances 0.000 description 12
- 238000002965 ELISA Methods 0.000 description 11
- 229940072221 immunoglobulins Drugs 0.000 description 11
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 11
- 229910002019 Aerosil® 380 Inorganic materials 0.000 description 10
- 239000008280 blood Substances 0.000 description 10
- 210000004369 blood Anatomy 0.000 description 10
- 230000007812 deficiency Effects 0.000 description 10
- 229940009600 gammagard Drugs 0.000 description 10
- 208000028529 primary immunodeficiency disease Diseases 0.000 description 10
- 238000003756 stirring Methods 0.000 description 10
- 239000011534 wash buffer Substances 0.000 description 10
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 9
- 239000006172 buffering agent Substances 0.000 description 9
- 238000009826 distribution Methods 0.000 description 9
- 235000019799 monosodium phosphate Nutrition 0.000 description 9
- 239000008213 purified water Substances 0.000 description 9
- 239000003153 chemical reaction reagent Substances 0.000 description 8
- 229910000403 monosodium phosphate Inorganic materials 0.000 description 8
- 235000002639 sodium chloride Nutrition 0.000 description 8
- 239000007787 solid Substances 0.000 description 8
- 201000010717 Bruton-type agammaglobulinemia Diseases 0.000 description 7
- 208000031981 Thrombocytopenic Idiopathic Purpura Diseases 0.000 description 7
- 102000004338 Transferrin Human genes 0.000 description 7
- 108090000901 Transferrin Proteins 0.000 description 7
- 201000006417 multiple sclerosis Diseases 0.000 description 7
- WWZKQHOCKIZLMA-UHFFFAOYSA-N octanoic acid Chemical compound CCCCCCCC(O)=O WWZKQHOCKIZLMA-UHFFFAOYSA-N 0.000 description 7
- 230000009467 reduction Effects 0.000 description 7
- 239000012134 supernatant fraction Substances 0.000 description 7
- 239000012581 transferrin Substances 0.000 description 7
- 206010000234 Abortion spontaneous Diseases 0.000 description 6
- 108010088751 Albumins Proteins 0.000 description 6
- 102000009027 Albumins Human genes 0.000 description 6
- 208000010839 B-cell chronic lymphocytic leukemia Diseases 0.000 description 6
- 208000030939 Chronic inflammatory demyelinating polyneuropathy Diseases 0.000 description 6
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 6
- 206010021245 Idiopathic thrombocytopenic purpura Diseases 0.000 description 6
- 208000031422 Lymphocytic Chronic B-Cell Leukemia Diseases 0.000 description 6
- 208000007400 Relapsing-Remitting Multiple Sclerosis Diseases 0.000 description 6
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 6
- 208000016349 X-linked agammaglobulinemia Diseases 0.000 description 6
- 201000003710 autoimmune thrombocytopenic purpura Diseases 0.000 description 6
- 201000005795 chronic inflammatory demyelinating polyneuritis Diseases 0.000 description 6
- 208000032852 chronic lymphocytic leukemia Diseases 0.000 description 6
- 230000001419 dependent effect Effects 0.000 description 6
- 208000027866 inflammatory disease Diseases 0.000 description 6
- 238000007726 management method Methods 0.000 description 6
- 229940045641 monobasic sodium phosphate Drugs 0.000 description 6
- 239000001632 sodium acetate Substances 0.000 description 6
- 235000017281 sodium acetate Nutrition 0.000 description 6
- 208000000995 spontaneous abortion Diseases 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- 239000004094 surface-active agent Substances 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 208000024827 Alzheimer disease Diseases 0.000 description 5
- 102000004506 Blood Proteins Human genes 0.000 description 5
- 108010017384 Blood Proteins Proteins 0.000 description 5
- 208000018737 Parkinson disease Diseases 0.000 description 5
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 5
- 229920001213 Polysorbate 20 Polymers 0.000 description 5
- 241000700605 Viruses Species 0.000 description 5
- 238000004587 chromatography analysis Methods 0.000 description 5
- 230000002779 inactivation Effects 0.000 description 5
- 230000002757 inflammatory effect Effects 0.000 description 5
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 5
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 5
- 239000011780 sodium chloride Substances 0.000 description 5
- 239000001509 sodium citrate Substances 0.000 description 5
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 5
- 238000003860 storage Methods 0.000 description 5
- 230000003612 virological effect Effects 0.000 description 5
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 4
- 239000008364 bulk solution Substances 0.000 description 4
- 229920002301 cellulose acetate Polymers 0.000 description 4
- 238000007796 conventional method Methods 0.000 description 4
- 230000007423 decrease Effects 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- 238000002955 isolation Methods 0.000 description 4
- 238000012423 maintenance Methods 0.000 description 4
- 239000003595 mist Substances 0.000 description 4
- 239000000178 monomer Substances 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 241000894007 species Species 0.000 description 4
- 239000011800 void material Substances 0.000 description 4
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- 208000008190 Agammaglobulinemia Diseases 0.000 description 3
- 239000005635 Caprylic acid (CAS 124-07-2) Substances 0.000 description 3
- LZZYPRNAOMGNLH-UHFFFAOYSA-M Cetrimonium bromide Chemical compound [Br-].CCCCCCCCCCCCCCCC[N+](C)(C)C LZZYPRNAOMGNLH-UHFFFAOYSA-M 0.000 description 3
- 206010008874 Chronic Fatigue Syndrome Diseases 0.000 description 3
- 206010009657 Clostridium difficile colitis Diseases 0.000 description 3
- 208000028399 Critical Illness Diseases 0.000 description 3
- 206010060742 Endocrine ophthalmopathy Diseases 0.000 description 3
- 208000007985 Erythema Infectiosum Diseases 0.000 description 3
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 208000035895 Guillain-Barré syndrome Diseases 0.000 description 3
- 206010020983 Hypogammaglobulinaemia Diseases 0.000 description 3
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 3
- 208000011200 Kawasaki disease Diseases 0.000 description 3
- 201000010743 Lambert-Eaton myasthenic syndrome Diseases 0.000 description 3
- 108090001030 Lipoproteins Proteins 0.000 description 3
- 102000004895 Lipoproteins Human genes 0.000 description 3
- 206010049567 Miller Fisher syndrome Diseases 0.000 description 3
- 208000034578 Multiple myelomas Diseases 0.000 description 3
- 208000009567 Neonatal Alloimmune Thrombocytopenia Diseases 0.000 description 3
- 206010053854 Opsoclonus myoclonus Diseases 0.000 description 3
- 208000005225 Opsoclonus-Myoclonus Syndrome Diseases 0.000 description 3
- 241000721454 Pemphigus Species 0.000 description 3
- 206010035226 Plasma cell myeloma Diseases 0.000 description 3
- 208000031951 Primary immunodeficiency Diseases 0.000 description 3
- 206010040047 Sepsis Diseases 0.000 description 3
- 206010040070 Septic Shock Diseases 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 206010042033 Stevens-Johnson syndrome Diseases 0.000 description 3
- 206010072148 Stiff-Person syndrome Diseases 0.000 description 3
- 206010044223 Toxic epidermal necrolysis Diseases 0.000 description 3
- 231100000087 Toxic epidermal necrolysis Toxicity 0.000 description 3
- 208000003441 Transfusion reaction Diseases 0.000 description 3
- 206010052779 Transplant rejections Diseases 0.000 description 3
- 239000013504 Triton X-100 Substances 0.000 description 3
- 229920004890 Triton X-100 Polymers 0.000 description 3
- 125000000217 alkyl group Chemical group 0.000 description 3
- 230000000735 allogeneic effect Effects 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 238000005349 anion exchange Methods 0.000 description 3
- 239000000427 antigen Substances 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 210000001185 bone marrow Anatomy 0.000 description 3
- 238000005341 cation exchange Methods 0.000 description 3
- 238000011178 cuno filtration Methods 0.000 description 3
- 238000011118 depth filtration Methods 0.000 description 3
- 201000001981 dermatomyositis Diseases 0.000 description 3
- 239000013024 dilution buffer Substances 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 239000012149 elution buffer Substances 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 239000000284 extract Substances 0.000 description 3
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 3
- 201000008319 inclusion body myositis Diseases 0.000 description 3
- 210000003734 kidney Anatomy 0.000 description 3
- 206010025135 lupus erythematosus Diseases 0.000 description 3
- 208000015994 miscarriage Diseases 0.000 description 3
- 238000012544 monitoring process Methods 0.000 description 3
- 208000001725 mucocutaneous lymph node syndrome Diseases 0.000 description 3
- 206010065579 multifocal motor neuropathy Diseases 0.000 description 3
- 201000006938 muscular dystrophy Diseases 0.000 description 3
- 208000029766 myalgic encephalomeyelitis/chronic fatigue syndrome Diseases 0.000 description 3
- 206010028417 myasthenia gravis Diseases 0.000 description 3
- VLKZOEOYAKHREP-UHFFFAOYSA-N n-Hexane Chemical compound CCCCCC VLKZOEOYAKHREP-UHFFFAOYSA-N 0.000 description 3
- WWZKQHOCKIZLMA-UHFFFAOYSA-M octanoate Chemical compound CCCCCCCC([O-])=O WWZKQHOCKIZLMA-UHFFFAOYSA-M 0.000 description 3
- 229960002446 octanoic acid Drugs 0.000 description 3
- HEGSGKPQLMEBJL-RKQHYHRCSA-N octyl beta-D-glucopyranoside Chemical compound CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O HEGSGKPQLMEBJL-RKQHYHRCSA-N 0.000 description 3
- 238000011020 pilot scale process Methods 0.000 description 3
- 229920001223 polyethylene glycol Polymers 0.000 description 3
- 208000005987 polymyositis Diseases 0.000 description 3
- 230000006920 protein precipitation Effects 0.000 description 3
- 230000036303 septic shock Effects 0.000 description 3
- 239000003381 stabilizer Substances 0.000 description 3
- 229910001220 stainless steel Inorganic materials 0.000 description 3
- 239000010935 stainless steel Substances 0.000 description 3
- 238000010257 thawing Methods 0.000 description 3
- 239000008215 water for injection Substances 0.000 description 3
- YFSUTJLHUFNCNZ-UHFFFAOYSA-M 1,1,2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-heptadecafluorooctane-1-sulfonate Chemical compound [O-]S(=O)(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)F YFSUTJLHUFNCNZ-UHFFFAOYSA-M 0.000 description 2
- 108010032597 Cohn fraction II Proteins 0.000 description 2
- 201000003874 Common Variable Immunodeficiency Diseases 0.000 description 2
- 241000651994 Curio Species 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 108010076282 Factor IX Proteins 0.000 description 2
- 108010054218 Factor VIII Proteins 0.000 description 2
- 102000001690 Factor VIII Human genes 0.000 description 2
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 2
- 102000006395 Globulins Human genes 0.000 description 2
- 108010044091 Globulins Proteins 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 208000003352 Hyper-IgM Immunodeficiency Syndrome Diseases 0.000 description 2
- 108090000113 Plasma Kallikrein Proteins 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-M Propionate Chemical compound CCC([O-])=O XBDQKXXYIPTUBI-UHFFFAOYSA-M 0.000 description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 229960000686 benzalkonium chloride Drugs 0.000 description 2
- 229960001950 benzethonium chloride Drugs 0.000 description 2
- UREZNYTWGJKWBI-UHFFFAOYSA-M benzethonium chloride Chemical compound [Cl-].C1=CC(C(C)(C)CC(C)(C)C)=CC=C1OCCOCC[N+](C)(C)CC1=CC=CC=C1 UREZNYTWGJKWBI-UHFFFAOYSA-M 0.000 description 2
- CADWTSSKOVRVJC-UHFFFAOYSA-N benzyl(dimethyl)azanium;chloride Chemical compound [Cl-].C[NH+](C)CC1=CC=CC=C1 CADWTSSKOVRVJC-UHFFFAOYSA-N 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
- 229960000074 biopharmaceutical Drugs 0.000 description 2
- 229960001927 cetylpyridinium chloride Drugs 0.000 description 2
- YMKDRGPMQRFJGP-UHFFFAOYSA-M cetylpyridinium chloride Chemical compound [Cl-].CCCCCCCCCCCCCCCC[N+]1=CC=CC=C1 YMKDRGPMQRFJGP-UHFFFAOYSA-M 0.000 description 2
- WOQQAWHSKSSAGF-WXFJLFHKSA-N decyl beta-D-maltopyranoside Chemical compound O[C@@H]1[C@@H](O)[C@H](OCCCCCCCCCC)O[C@H](CO)[C@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 WOQQAWHSKSSAGF-WXFJLFHKSA-N 0.000 description 2
- 238000004925 denaturation Methods 0.000 description 2
- 230000036425 denaturation Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 239000012467 final product Substances 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 229960002737 fructose Drugs 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 108010074605 gamma-Globulins Proteins 0.000 description 2
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 2
- BXWNKGSJHAJOGX-UHFFFAOYSA-N hexadecan-1-ol Chemical compound CCCCCCCCCCCCCCCCO BXWNKGSJHAJOGX-UHFFFAOYSA-N 0.000 description 2
- 206010066130 hyper-IgM syndrome Diseases 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000003960 organic solvent Substances 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 229920001983 poloxamer Polymers 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 229910000162 sodium phosphate Inorganic materials 0.000 description 2
- 230000000087 stabilizing effect Effects 0.000 description 2
- HHVIBTZHLRERCL-UHFFFAOYSA-N sulfonyldimethane Chemical compound CS(C)(=O)=O HHVIBTZHLRERCL-UHFFFAOYSA-N 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 230000001052 transient effect Effects 0.000 description 2
- STCOOQWBFONSKY-UHFFFAOYSA-N tributyl phosphate Chemical compound CCCCOP(=O)(OCCCC)OCCCC STCOOQWBFONSKY-UHFFFAOYSA-N 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 239000013621 viresolve pro solution Substances 0.000 description 2
- UDPGUMQDCGORJQ-UHFFFAOYSA-N (2-chloroethyl)phosphonic acid Chemical compound OP(O)(=O)CCCl UDPGUMQDCGORJQ-UHFFFAOYSA-N 0.000 description 1
- ALSTYHKOOCGGFT-KTKRTIGZSA-N (9Z)-octadecen-1-ol Chemical compound CCCCCCCC\C=C/CCCCCCCCO ALSTYHKOOCGGFT-KTKRTIGZSA-N 0.000 description 1
- GYSCBCSGKXNZRH-UHFFFAOYSA-N 1-benzothiophene-2-carboxamide Chemical compound C1=CC=C2SC(C(=O)N)=CC2=C1 GYSCBCSGKXNZRH-UHFFFAOYSA-N 0.000 description 1
- SNGREZUHAYWORS-UHFFFAOYSA-M 2,2,3,3,4,4,5,5,6,6,7,7,8,8,8-pentadecafluorooctanoate Chemical compound [O-]C(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)F SNGREZUHAYWORS-UHFFFAOYSA-M 0.000 description 1
- AWQSAIIDOMEEOD-UHFFFAOYSA-N 5,5-Dimethyl-4-(3-oxobutyl)dihydro-2(3H)-furanone Chemical compound CC(=O)CCC1CC(=O)OC1(C)C AWQSAIIDOMEEOD-UHFFFAOYSA-N 0.000 description 1
- ADHFMENDOUEJRK-UHFFFAOYSA-N 9-[(4-fluorophenyl)methyl]-n-hydroxypyrido[3,4-b]indole-3-carboxamide Chemical compound C1=NC(C(=O)NO)=CC(C2=CC=CC=C22)=C1N2CC1=CC=C(F)C=C1 ADHFMENDOUEJRK-UHFFFAOYSA-N 0.000 description 1
- 206010067484 Adverse reaction Diseases 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-M Aminoacetate Chemical compound NCC([O-])=O DHMQDGOQFOQNFH-UHFFFAOYSA-M 0.000 description 1
- 102000004881 Angiotensinogen Human genes 0.000 description 1
- 108090001067 Angiotensinogen Proteins 0.000 description 1
- 208000003508 Botulism Diseases 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 108010075016 Ceruloplasmin Proteins 0.000 description 1
- 102100023321 Ceruloplasmin Human genes 0.000 description 1
- 102000003914 Cholinesterases Human genes 0.000 description 1
- 108090000322 Cholinesterases Proteins 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 206010010099 Combined immunodeficiency Diseases 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- RGHNJXZEOKUKBD-SQOUGZDYSA-M D-gluconate Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O RGHNJXZEOKUKBD-SQOUGZDYSA-M 0.000 description 1
- GHVNFZFCNZKVNT-UHFFFAOYSA-N Decanoic acid Natural products CCCCCCCCCC(O)=O GHVNFZFCNZKVNT-UHFFFAOYSA-N 0.000 description 1
- QRLVDLBMBULFAL-UHFFFAOYSA-N Digitonin Natural products CC1CCC2(OC1)OC3C(O)C4C5CCC6CC(OC7OC(CO)C(OC8OC(CO)C(O)C(OC9OCC(O)C(O)C9OC%10OC(CO)C(O)C(OC%11OC(CO)C(O)C(O)C%11O)C%10O)C8O)C(O)C7O)C(O)CC6(C)C5CCC4(C)C3C2C QRLVDLBMBULFAL-UHFFFAOYSA-N 0.000 description 1
- 108010071241 Factor XIIa Proteins 0.000 description 1
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 0.000 description 1
- 229930091371 Fructose Natural products 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- 102000013271 Hemopexin Human genes 0.000 description 1
- 108010026027 Hemopexin Proteins 0.000 description 1
- 101000837639 Homo sapiens Thyroxine-binding globulin Proteins 0.000 description 1
- 208000028622 Immune thrombocytopenia Diseases 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- FEWJPZIEWOKRBE-JCYAYHJZSA-L L-tartrate(2-) Chemical compound [O-]C(=O)[C@H](O)[C@@H](O)C([O-])=O FEWJPZIEWOKRBE-JCYAYHJZSA-L 0.000 description 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 108090000581 Leukemia inhibitory factor Proteins 0.000 description 1
- 102100032352 Leukemia inhibitory factor Human genes 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000204801 Muraenidae Species 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 208000025966 Neurological disease Diseases 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108010081690 Pertussis Toxin Proteins 0.000 description 1
- 241001482237 Pica Species 0.000 description 1
- RVGRUAULSDPKGF-UHFFFAOYSA-N Poloxamer Chemical compound C1CO1.CC1CO1 RVGRUAULSDPKGF-UHFFFAOYSA-N 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 206010037742 Rabies Diseases 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 206010057863 Selective IgG subclass deficiency Diseases 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 108010055044 Tetanus Toxin Proteins 0.000 description 1
- 102100028709 Thyroxine-binding globulin Human genes 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- KXKVLQRXCPHEJC-UHFFFAOYSA-N acetic acid trimethyl ester Natural products COC(C)=O KXKVLQRXCPHEJC-UHFFFAOYSA-N 0.000 description 1
- PNZVFASWDSMJER-UHFFFAOYSA-N acetic acid;lead Chemical compound [Pb].CC(O)=O PNZVFASWDSMJER-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000010306 acid treatment Methods 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000006838 adverse reaction Effects 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000004996 alkyl benzenes Chemical class 0.000 description 1
- 125000005211 alkyl trimethyl ammonium group Chemical group 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 229940024606 amino acid Drugs 0.000 description 1
- BTBJBAZGXNKLQC-UHFFFAOYSA-N ammonium lauryl sulfate Chemical compound [NH4+].CCCCCCCCCCCCOS([O-])(=O)=O BTBJBAZGXNKLQC-UHFFFAOYSA-N 0.000 description 1
- 229940063953 ammonium lauryl sulfate Drugs 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 239000003957 anion exchange resin Substances 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000004019 antithrombin Substances 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 229940077388 benzenesulfonate Drugs 0.000 description 1
- WPYMKLBDIGXBTP-UHFFFAOYSA-N benzoic acid Chemical compound OC(=O)C1=CC=CC=C1 WPYMKLBDIGXBTP-UHFFFAOYSA-N 0.000 description 1
- GONOPSZTUGRENK-UHFFFAOYSA-N benzyl(trichloro)silane Chemical compound Cl[Si](Cl)(Cl)CC1=CC=CC=C1 GONOPSZTUGRENK-UHFFFAOYSA-N 0.000 description 1
- 229940126587 biotherapeutics Drugs 0.000 description 1
- OHJMTUPIZMNBFR-UHFFFAOYSA-N biuret Chemical compound NC(=O)NC(N)=O OHJMTUPIZMNBFR-UHFFFAOYSA-N 0.000 description 1
- 229960000182 blood factors Drugs 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 235000001465 calcium Nutrition 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 101150039352 can gene Proteins 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 229960000541 cetyl alcohol Drugs 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 229940048961 cholinesterase Drugs 0.000 description 1
- 238000011210 chromatographic step Methods 0.000 description 1
- MRUAUOIMASANKQ-UHFFFAOYSA-N cocamidopropyl betaine Chemical compound CCCCCCCCCCCC(=O)NCCC[N+](C)(C)CC([O-])=O MRUAUOIMASANKQ-UHFFFAOYSA-N 0.000 description 1
- 229940073507 cocamidopropyl betaine Drugs 0.000 description 1
- 239000000084 colloidal system Substances 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 238000013329 compounding Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 238000004690 coupled electron pair approximation Methods 0.000 description 1
- 238000009295 crossflow filtration Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 239000012471 diafiltration solution Substances 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- UVYVLBIGDKGWPX-KUAJCENISA-N digitonin Chemical compound O([C@@H]1[C@@H]([C@]2(CC[C@@H]3[C@@]4(C)C[C@@H](O)[C@H](O[C@H]5[C@@H]([C@@H](O)[C@@H](O[C@H]6[C@@H]([C@@H](O[C@H]7[C@@H]([C@@H](O)[C@H](O)CO7)O)[C@H](O)[C@@H](CO)O6)O[C@H]6[C@@H]([C@@H](O[C@H]7[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O7)O)[C@@H](O)[C@@H](CO)O6)O)[C@@H](CO)O5)O)C[C@@H]4CC[C@H]3[C@@H]2[C@@H]1O)C)[C@@H]1C)[C@]11CC[C@@H](C)CO1 UVYVLBIGDKGWPX-KUAJCENISA-N 0.000 description 1
- UVYVLBIGDKGWPX-UHFFFAOYSA-N digitonine Natural products CC1C(C2(CCC3C4(C)CC(O)C(OC5C(C(O)C(OC6C(C(OC7C(C(O)C(O)CO7)O)C(O)C(CO)O6)OC6C(C(OC7C(C(O)C(O)C(CO)O7)O)C(O)C(CO)O6)O)C(CO)O5)O)CC4CCC3C2C2O)C)C2OC11CCC(C)CO1 UVYVLBIGDKGWPX-UHFFFAOYSA-N 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- SMVRDGHCVNAOIN-UHFFFAOYSA-L disodium;1-dodecoxydodecane;sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O.CCCCCCCCCCCCOCCCCCCCCCCCC SMVRDGHCVNAOIN-UHFFFAOYSA-L 0.000 description 1
- 238000011978 dissolution method Methods 0.000 description 1
- SYELZBGXAIXKHU-UHFFFAOYSA-N dodecyldimethylamine N-oxide Chemical compound CCCCCCCCCCCC[N+](C)(C)[O-] SYELZBGXAIXKHU-UHFFFAOYSA-N 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 238000011143 downstream manufacturing Methods 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 150000002191 fatty alcohols Chemical class 0.000 description 1
- 230000020764 fibrinolysis Effects 0.000 description 1
- 239000013020 final formulation Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 229940044170 formate Drugs 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229940050410 gluconate Drugs 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- MNWFXJYAOYHMED-UHFFFAOYSA-N heptanoic acid Chemical compound CCCCCCC(O)=O MNWFXJYAOYHMED-UHFFFAOYSA-N 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 239000007970 homogeneous dispersion Substances 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 230000002706 hydrostatic effect Effects 0.000 description 1
- XJFQCYIFOWHHFN-PLKCGDGVSA-N hypertensinogen Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C1=CC=C(O)C=C1 XJFQCYIFOWHHFN-PLKCGDGVSA-N 0.000 description 1
- 208000026278 immune system disease Diseases 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 239000002563 ionic surfactant Substances 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 150000004668 long chain fatty acids Chemical class 0.000 description 1
- 238000009115 maintenance therapy Methods 0.000 description 1
- 229940049920 malate Drugs 0.000 description 1
- BJEPYKJPYRNKOW-UHFFFAOYSA-L malate(2-) Chemical compound [O-]C(=O)C(O)CC([O-])=O BJEPYKJPYRNKOW-UHFFFAOYSA-L 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000005374 membrane filtration Methods 0.000 description 1
- 235000010755 mineral Nutrition 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- DVEKCXOJTLDBFE-UHFFFAOYSA-N n-dodecyl-n,n-dimethylglycinate Chemical compound CCCCCCCCCCCC[N+](C)(C)CC([O-])=O DVEKCXOJTLDBFE-UHFFFAOYSA-N 0.000 description 1
- FUZZWVXGSFPDMH-UHFFFAOYSA-N n-hexanoic acid Natural products CCCCCC(O)=O FUZZWVXGSFPDMH-UHFFFAOYSA-N 0.000 description 1
- 230000000926 neurological effect Effects 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- YYELLDKEOUKVIQ-UHFFFAOYSA-N octaethyleneglycol monododecyl ether Chemical compound CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCO YYELLDKEOUKVIQ-UHFFFAOYSA-N 0.000 description 1
- 229940055577 oleyl alcohol Drugs 0.000 description 1
- XMLQWXUVTXCDDL-UHFFFAOYSA-N oleyl alcohol Natural products CCCCCCC=CCCCCCCCCCCO XMLQWXUVTXCDDL-UHFFFAOYSA-N 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 238000013386 optimize process Methods 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 239000006174 pH buffer Substances 0.000 description 1
- SNGREZUHAYWORS-UHFFFAOYSA-N perfluorooctanoic acid Chemical compound OC(=O)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)C(F)(F)F SNGREZUHAYWORS-UHFFFAOYSA-N 0.000 description 1
- 108010055837 phosphocarrier protein HPr Proteins 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 238000001470 plasma protein fractionation Methods 0.000 description 1
- 238000002616 plasmapheresis Methods 0.000 description 1
- 229960000502 poloxamer Drugs 0.000 description 1
- 229920001987 poloxamine Polymers 0.000 description 1
- 229920006393 polyether sulfone Polymers 0.000 description 1
- 229920001451 polypropylene glycol Polymers 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229940068977 polysorbate 20 Drugs 0.000 description 1
- 229940068965 polysorbates Drugs 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 229940024790 prothrombin complex concentrate Drugs 0.000 description 1
- 238000010926 purge Methods 0.000 description 1
- 238000005067 remediation Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 239000012465 retentate Substances 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 229940057950 sodium laureth sulfate Drugs 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 235000011008 sodium phosphates Nutrition 0.000 description 1
- SXHLENDCVBIJFO-UHFFFAOYSA-M sodium;2-[2-(2-dodecoxyethoxy)ethoxy]ethyl sulfate Chemical compound [Na+].CCCCCCCCCCCCOCCOCCOCCOS([O-])(=O)=O SXHLENDCVBIJFO-UHFFFAOYSA-M 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 229940086735 succinate Drugs 0.000 description 1
- KDYFGRWQOYBRFD-UHFFFAOYSA-L succinate(2-) Chemical compound [O-]C(=O)CCC([O-])=O KDYFGRWQOYBRFD-UHFFFAOYSA-L 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 239000003760 tallow Substances 0.000 description 1
- 229940095064 tartrate Drugs 0.000 description 1
- 229940118376 tetanus toxin Drugs 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 238000010977 unit operation Methods 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 239000013579 wash concentrate Substances 0.000 description 1
- 239000002888 zwitterionic surfactant Substances 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
- A61K35/14—Blood; Artificial blood
- A61K35/16—Blood plasma; Blood serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
- A61K38/57—Protease inhibitors from animals; from humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39516—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum from serum, plasma
- A61K39/39525—Purification
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/06—Organic compounds, e.g. natural or synthetic hydrocarbons, polyolefins, mineral oil, petrolatum or ozokerite
- A61K47/16—Organic compounds, e.g. natural or synthetic hydrocarbons, polyolefins, mineral oil, petrolatum or ozokerite containing nitrogen, e.g. nitro-, nitroso-, azo-compounds, nitriles, cyanates
- A61K47/18—Amines; Amides; Ureas; Quaternary ammonium compounds; Amino acids; Oligopeptides having up to five amino acids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/06—Organic compounds, e.g. natural or synthetic hydrocarbons, polyolefins, mineral oil, petrolatum or ozokerite
- A61K47/16—Organic compounds, e.g. natural or synthetic hydrocarbons, polyolefins, mineral oil, petrolatum or ozokerite containing nitrogen, e.g. nitro-, nitroso-, azo-compounds, nitriles, cyanates
- A61K47/18—Amines; Amides; Ureas; Quaternary ammonium compounds; Amino acids; Oligopeptides having up to five amino acids
- A61K47/183—Amino acids, e.g. glycine, EDTA or aspartame
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0019—Injectable compositions; Intramuscular, intravenous, arterial, subcutaneous administration; Compositions to be administered through the skin in an invasive manner
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0019—Injectable compositions; Intramuscular, intravenous, arterial, subcutaneous administration; Compositions to be administered through the skin in an invasive manner
- A61K9/0026—Blood substitute; Oxygen transporting formulations; Plasma extender
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/08—Solutions
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/10—Selective adsorption, e.g. chromatography characterised by constructional or operational features
- B01D15/12—Selective adsorption, e.g. chromatography characterised by constructional or operational features relating to the preparation of the feed
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/36—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
- B01D15/361—Ion-exchange
- B01D15/362—Cation-exchange
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/36—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving ionic interaction, e.g. ion-exchange, ion-pair, ion-suppression or ion-exclusion
- B01D15/361—Ion-exchange
- B01D15/363—Anion-exchange
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/42—Selective adsorption, e.g. chromatography characterised by the development mode, e.g. by displacement or by elution
- B01D15/424—Elution mode
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J20/00—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof
- B01J20/02—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof comprising inorganic material
- B01J20/10—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof comprising inorganic material comprising silica or silicate
-
- 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
- C07K1/30—Extraction; Separation; Purification by precipitation
-
- 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
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/18—Ion-exchange chromatography
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Epidemiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Chemical & Material Sciences (AREA)
- Analytical Chemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Hematology (AREA)
- Zoology (AREA)
- Cell Biology (AREA)
- Gastroenterology & Hepatology (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Biomedical Technology (AREA)
- Dermatology (AREA)
- Virology (AREA)
- Developmental Biology & Embryology (AREA)
- Biotechnology (AREA)
- Marine Sciences & Fisheries (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Diabetes (AREA)
- Oncology (AREA)
- Transplantation (AREA)
- Inorganic Chemistry (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2010202125 | 2010-05-26 | ||
| AU2010202125A AU2010202125B1 (en) | 2010-05-26 | 2010-05-26 | A method to produce an immunoglobulin preparation with improved yield |
| PCT/US2010/036470 WO2011149472A1 (en) | 2010-05-26 | 2010-05-27 | Method for preparing an enriched igg composition from plasma |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2800155A1 true CA2800155A1 (en) | 2011-12-01 |
Family
ID=42727304
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2800155A Abandoned CA2800155A1 (en) | 2010-05-26 | 2010-05-27 | Method for preparing an enriched igg composition from plasma |
| CA2800272A Abandoned CA2800272A1 (en) | 2010-05-26 | 2011-05-26 | Removal of serine proteases by treatment with finely divided silicon dioxide |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2800272A Abandoned CA2800272A1 (en) | 2010-05-26 | 2011-05-26 | Removal of serine proteases by treatment with finely divided silicon dioxide |
Country Status (25)
| Country | Link |
|---|---|
| US (6) | US8993734B2 (enExample) |
| EP (6) | EP2803349B1 (enExample) |
| JP (6) | JP5876474B2 (enExample) |
| KR (3) | KR101647617B1 (enExample) |
| CN (5) | CN104958761B (enExample) |
| AR (4) | AR076800A1 (enExample) |
| AU (8) | AU2010202125B1 (enExample) |
| BR (2) | BR112012029893B1 (enExample) |
| CA (2) | CA2800155A1 (enExample) |
| CL (3) | CL2012003290A1 (enExample) |
| CO (2) | CO6660439A2 (enExample) |
| DK (3) | DK2554160T3 (enExample) |
| EA (4) | EA023446B1 (enExample) |
| ES (4) | ES2959234T3 (enExample) |
| HK (1) | HK1213790A1 (enExample) |
| HR (3) | HRP20141109T1 (enExample) |
| HU (1) | HUE064400T2 (enExample) |
| IL (2) | IL223150A0 (enExample) |
| MX (4) | MX364252B (enExample) |
| MY (3) | MY160551A (enExample) |
| PL (4) | PL2445482T3 (enExample) |
| PT (3) | PT2445482E (enExample) |
| SG (3) | SG185724A1 (enExample) |
| TW (3) | TWI531577B (enExample) |
| WO (1) | WO2011149472A1 (enExample) |
Families Citing this family (57)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TWI489994B (zh) | 2008-03-17 | 2015-07-01 | Baxter Healthcare Sa | 供免疫球蛋白及玻尿酸酶之皮下投藥之用的組合及方法 |
| US9084743B2 (en) * | 2009-09-17 | 2015-07-21 | Baxter International Inc. | Stable co-formulation of hyaluronidase and immunoglobulin, and methods of use thereof |
| US10787701B2 (en) | 2010-04-05 | 2020-09-29 | Prognosys Biosciences, Inc. | Spatially encoded biological assays |
| WO2011150284A2 (en) | 2010-05-26 | 2011-12-01 | Baxter International Inc. | Removal of serine proteases by treatment with finely divided silicon dioxide |
| AU2010202125B1 (en) | 2010-05-26 | 2010-09-02 | Takeda Pharmaceutical Company Limited | A method to produce an immunoglobulin preparation with improved yield |
| US8841248B2 (en) * | 2010-07-23 | 2014-09-23 | Baxter International Inc. | Manufacture of inter-alpha-inhibitor (IaIp) from plasma |
| AU2011364724B2 (en) * | 2011-04-08 | 2016-11-17 | Universidad De Costa Rica | Method for producing injectable formulations of blood-derived protein materials, and materials obtained using said method |
| PT2791675T (pt) | 2011-12-13 | 2018-07-27 | Baxalta Inc | Medição de autoanticorpos em condições de baixa condutividade |
| TWI629283B (zh) * | 2012-02-23 | 2018-07-11 | 巴克斯歐塔公司 | 來自血漿中的免疫球蛋白之ｉ-ｉｖ-１部分沉澱 |
| RU2487725C1 (ru) * | 2012-03-15 | 2013-07-20 | Федеральное государственное унитарное предприятие "Научно-производственное объединение по медицинским иммунобиологическим препаратам "Микроген" Министерства здравоохранения Российской Федерации (ФГУП "НПО "Микроген" Минздрава России) | Способ получения концентрированного иммуноглобулинового препарата для подкожного введения |
| CN103197053B (zh) * | 2013-03-15 | 2015-02-18 | 上海市血液中心 | 一种抗IgA抗体检测试剂盒 |
| AU2013203043B2 (en) * | 2013-03-15 | 2016-10-06 | Takeda Pharmaceutical Company Limited | Methods to produce a human plasma-derived igg preparation enriched in brain disease-related natural iggs |
| CN104086646B (zh) * | 2014-07-03 | 2018-10-09 | 成都蓉生药业有限责任公司 | 血液制品中fv沉淀的制备方法 |
| CN104086642A (zh) * | 2014-07-03 | 2014-10-08 | 成都蓉生药业有限责任公司 | 血液制品中fi+iii上清的制备方法 |
| CN104072601A (zh) * | 2014-07-03 | 2014-10-01 | 成都蓉生药业有限责任公司 | 血液制品中fii沉淀的制备方法 |
| GB201413227D0 (en) * | 2014-07-25 | 2014-09-10 | Bioproducts Lab Ltd | Process |
| WO2016064955A1 (en) | 2014-10-21 | 2016-04-28 | The General Hospital Corporation | Methods of diagnosis and treatment of tuberculosis and infection |
| CN204424090U (zh) | 2014-11-28 | 2015-06-24 | 比亚迪股份有限公司 | 薄膜电容器 |
| US10583179B2 (en) * | 2015-04-02 | 2020-03-10 | Kieu Hoang | Method of manufacturing and purifying prothrombin complex concentrate from Fraction III for intravenous injection and a method of curing and preventing Hemophilia A with inhibitors or Hemophilia B in patients infected with HIV-1 and HIV-2 |
| CN107921079A (zh) * | 2015-04-02 | 2018-04-17 | K·黄 | 由组分iii制造静脉注射免疫球蛋白的方法 |
| WO2016161423A1 (en) * | 2015-04-02 | 2016-10-06 | Kieu Hoang | Process of cloning and further purification to make a recombinant intravenous immunoglobulin |
| CN108495860A (zh) * | 2015-09-29 | 2018-09-04 | K·黄 | 一种从组分iii制备静脉注射免疫球蛋白的方法 |
| WO2017062536A2 (en) * | 2015-10-06 | 2017-04-13 | Kieu Hoang | A method of manfacturing prothrombin complex concentrate from fraction iii and non-prothrombin complex concentrate from fraction iv |
| CN106800583A (zh) * | 2015-11-26 | 2017-06-06 | 上海洲跃生物科技有限公司 | 一种速溶无析出的冻干人纤维蛋白原制备工艺 |
| EP3275897A1 (en) * | 2016-07-27 | 2018-01-31 | Biotest AG | Process for preparing immunoglobulin compositions |
| WO2018050872A1 (en) | 2016-09-16 | 2018-03-22 | Leukocare Ag | A novel method for obtaining efficient viral vector-based compositions for vaccination or gene therapy |
| JP7170329B2 (ja) * | 2016-09-16 | 2022-11-14 | ロイコケア・アクチェンゲゼルシャフト | 処理中の生物医薬製品の安定化のための新規な方法 |
| WO2018050873A1 (en) | 2016-09-16 | 2018-03-22 | Leukocare Ag | A novel method for producing low viscous and highly concentrated biopharmaceutical drug products in liquid formulation |
| US10259865B2 (en) | 2017-03-15 | 2019-04-16 | Adma Biologics, Inc. | Anti-pneumococcal hyperimmune globulin for the treatment and prevention of pneumococcal infection |
| CN110831627A (zh) * | 2017-04-21 | 2020-02-21 | 瑞士杰特贝林生物制品有限公司 | 用于治疗慢性炎症性脱髓鞘性多发性神经病的免疫球蛋白产品 |
| CA3080656A1 (en) | 2017-10-30 | 2019-05-09 | Baxalta GmbH | Environmentally compatible detergents for inactivation of lipid-enveloped viruses |
| WO2019121846A1 (en) * | 2017-12-19 | 2019-06-27 | CSL Behring Lengnau AG | Protein purification and virus inactivation with alkyl glycosides |
| WO2019199476A1 (en) * | 2018-04-12 | 2019-10-17 | Amgen Inc. | Methods for making stable protein compositions |
| CN108733099B (zh) * | 2018-05-31 | 2020-08-11 | 上海药明生物技术有限公司 | 低pH孵育和中和的自动调节系统及方法 |
| WO2021072137A1 (en) * | 2019-10-11 | 2021-04-15 | Baxalta Incorporated | Heparin-insensitive assay for factor xla |
| CN114667151B (zh) * | 2019-11-04 | 2025-05-23 | 万能溶剂有限公司 | 用于肌肉再生的血浆级分 |
| IL293121A (en) * | 2019-11-20 | 2022-07-01 | Csl Behring Ag | Method for extracting a protein from a precipitate and method for precipitating impurities |
| CA3173539A1 (en) * | 2020-03-31 | 2021-10-07 | Takeda Pharmaceutical Company Limited | A method to produce an immunoglobulin preparation from c-1 inhibitor depleted plasma |
| EP4118108A4 (en) | 2020-04-10 | 2024-05-15 | Plasma Technologies, LLC | COMPOSITIONS AND METHODS FOR HIGHLY EFFICIENT SIMPLIFIED PROTEIN ISOLATION |
| CN111961130B (zh) * | 2020-08-31 | 2021-09-10 | 华兰生物工程重庆有限公司 | 一种从血浆中提取并分离IgM和IgG的方法 |
| EP4222161A1 (en) * | 2020-10-01 | 2023-08-09 | Takeda Pharmaceutical Company Limited | Plasma fractionation process utilizing spray-dried human plasma |
| EP4271706A4 (en) | 2020-12-28 | 2025-01-15 | Plasma Technologies LLC | SYSTEMS AND METHODS FOR THE ISOLATION OF IMMUNGLOBULIN G ON A PROCESS SCALE |
| CN112574296B (zh) * | 2020-12-30 | 2023-05-19 | 中国医学科学院输血研究所 | 一种模拟IVIg的多人份混合人血浆IgG样品的分离纯化方法 |
| EP4377361A1 (en) | 2021-07-29 | 2024-06-05 | CSL Behring AG | Method of purifying immunoglobulin g and uses thereof |
| CA3236213A1 (en) | 2021-10-27 | 2023-05-04 | Eugene ZURLO | Compositions and methods for isolating proteins |
| KR102779378B1 (ko) * | 2022-01-05 | 2025-03-12 | 한양대학교 에리카산학협력단 | 1-알릴이소크로만 유도체와 이의 제조방법 |
| KR20230121373A (ko) * | 2022-02-11 | 2023-08-18 | 주식회사 녹십자 | 인자 xiii의 정제방법 |
| EP4490179A1 (en) | 2022-03-07 | 2025-01-15 | Takeda Pharmaceutical Company Limited | Affinity chromatographic production of clinical human igg products |
| EP4490042A1 (en) | 2022-03-08 | 2025-01-15 | Equashield Medical Ltd. | Fluid transfer station in a robotic pharmaceutical preparation system |
| JP2025514479A (ja) | 2022-05-02 | 2025-05-02 | 武田薬品工業株式会社 | 血漿から限外濾過によりコーンプール濃縮物を調製する方法 |
| AR129690A1 (es) | 2022-06-22 | 2024-09-18 | Ageronix SA | a1-ANTITRIPSINA PARA SU USO EN EL TRATAMIENTO DE ENFERMEDADES O TRASTORNOS DEL SISTEMA NERVIOSO COMO LA POLINEUROPATÍA DESMIELINIZANTE INFLAMATORIA CRÓNICA Y UN KIT |
| WO2024200757A1 (en) | 2023-03-29 | 2024-10-03 | Csl Behring Ag | Methods of identifying immunoglobulin associated with adverse reactions |
| WO2025008781A1 (en) | 2023-07-04 | 2025-01-09 | Csl Behring Ag | Method of purification |
| WO2025068923A2 (en) | 2023-09-26 | 2025-04-03 | Takeda Pharmaceutical Company Limited | IMMUNOGLOBULIN FORMULATIONS DEPLETED IN IgA |
| WO2025085544A1 (en) * | 2023-10-17 | 2025-04-24 | Plasma Technologies, Llc | Integrated process for isolation of plasma proteins |
| PL448469A1 (pl) * | 2024-04-30 | 2025-11-03 | Deveris Polska Spółka Z Ograniczoną Odpowiedzialnością | Przedmiotem wynalazku jest sposób wzbogacania preparatów plazmy krwi drobiowej w immunoglobulinę G (IgG) |
| WO2025229607A1 (en) | 2024-05-03 | 2025-11-06 | Csl Behring Ag | Systems and methods for solid-liquid separation |
Family Cites Families (89)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US2390074A (en) * | 1942-02-09 | 1945-12-04 | Research Corp | Protein product and process |
| SE348942B (enExample) | 1970-06-02 | 1972-09-18 | Statens Bakteriologiska Labor | |
| US4056614A (en) | 1972-09-22 | 1977-11-01 | Marc Bonneau | Immunity depressant medicine |
| US3998946A (en) * | 1975-04-23 | 1976-12-21 | The Regents Of The University Of Minnesota | Fibrinogen-free plasminogen-plasmin-free plasma and method of preparing and using same |
| DE2801123C2 (de) * | 1977-01-26 | 1986-01-02 | Armour Pharma GmbH & Co KG, 3440 Eschwege | Verfahren zur Herstellung eines intravenös applizierbaren Serumeiweiß-Präparates |
| US4136094A (en) | 1977-08-31 | 1979-01-23 | The Regents Of The University Of Minnesota | Preparation of intravenous human and animal gamma globulins and isolation of albumin |
| US4296027A (en) | 1977-08-31 | 1981-10-20 | The Regents Of The University Of Minnesota | Pure intravenous human and animal gamma globulins |
| US4357272A (en) * | 1978-03-22 | 1982-11-02 | The South African Inventions Development Corporation | Recovering purified antibodies from egg yolk |
| US4550019A (en) * | 1978-03-22 | 1985-10-29 | South Africa Inventions Development Corporation | Manufacture and use of fowl egg antibodies |
| DE2901822A1 (de) * | 1979-01-18 | 1980-07-31 | Biotest Serum Institut Gmbh | Verfahren zur herstellung einer fuer die intravenoese applikation geeigneten immunglobulinloesung, die igm in ankonzentrierter form enthaelt |
| DE2902158A1 (de) | 1979-01-20 | 1980-07-31 | Biotest Serum Institut Gmbh | Verfahren zur herstellung von fibrinogen, einem die gerinnungsfaktoren ii, vii, ix und x enthaltenden prothrombinkomplex, antithrombin iii und einer loesung von lagerstabilen serumproteinen |
| US4228154A (en) | 1979-02-26 | 1980-10-14 | Armour Pharmaceutical Company | Purification of plasma albumin by ion exchange chromatography |
| US4378346A (en) * | 1979-08-15 | 1983-03-29 | Tankersley Donald L | Intravenously injectable solution of plasma protein fraction free from bradykinin, kininogen and prekallikrein activators and processes for its production |
| US4499073A (en) * | 1981-08-24 | 1985-02-12 | Cutter Laboratories, Inc. | Intravenously injectable immune serum globulin |
| JPS5855432A (ja) | 1981-09-29 | 1983-04-01 | Fujirebio Inc | 静脈注射用免疫グロブリンの製法 |
| US4439358A (en) | 1982-06-17 | 1984-03-27 | Miles Laboratories, Inc. | Method of preparing alpha-1-proteinase inhibitor |
| US4624780A (en) | 1982-06-28 | 1986-11-25 | Alpha Therapeutic Corporation | Fractionation of blood plasma |
| DE3247150A1 (de) | 1982-12-21 | 1984-06-28 | Biotest-Serum-Institut Gmbh, 6000 Frankfurt | Gerinnungsaktive plasmaproteinloesung, verfahren zu ihrer herstellung und ihre verwendung zur behandlung von stoerungen des haemostasesystems |
| DK166763C (da) | 1983-03-16 | 1993-07-12 | Immuno Ag | Immunoglobulin-g-holdig fraktion |
| DE3523615A1 (de) | 1985-07-02 | 1987-01-15 | Cytomed Medizintechnik | Medizinisches geraet, insbesondere kanuele, katheter oder implantat |
| US5061237A (en) | 1985-07-02 | 1991-10-29 | Cytomed Medizintechnik Gmbh | Method of purifying whole blood |
| JPH0742235B2 (ja) | 1985-11-08 | 1995-05-10 | 三共株式会社 | 自己免疫性疾病の予防・治療剤 |
| US5136094A (en) | 1988-03-10 | 1992-08-04 | Air Products And Chemicals, Inc. | Process for the synthesis of secondary formamides |
| US5055447A (en) | 1988-07-28 | 1991-10-08 | Genentech, Inc. | Method and compositions for the treatment and prevention of septic shock |
| JP2871709B2 (ja) | 1988-11-21 | 1999-03-17 | 住友製薬株式会社 | 免疫グロブリンｇ結合活性を有する新規な蛋白質プロテインｈ、該蛋白質をコードする遺伝子及び該蛋白質の製造法 |
| US5177194A (en) | 1990-02-01 | 1993-01-05 | Baxter International, Inc. | Process for purifying immune serum globulins |
| EP0440509A3 (en) * | 1990-02-02 | 1991-12-18 | Common Services Agency | Novel cell growth medium components and process for producing same |
| ES2074490T5 (es) * | 1990-03-22 | 2004-02-16 | Biotest Pharma Gmbh | Procedimiento para la elaboracion de un preparado de inmunoglobulina g tolerable por via intravenosa. |
| US5130451A (en) * | 1991-03-28 | 1992-07-14 | Amoco Corporation | Process for preparing carboxyaryl phosphates |
| US5324425A (en) * | 1992-08-26 | 1994-06-28 | Ellison Billy L | Method and apparatus for removing solids from aqueous wash solutions |
| FR2706466B1 (fr) | 1993-06-14 | 1995-08-25 | Aetsrn | Concentré d'immunoglobulines G à usage thérapeutique et procédé de production dudit concentré. |
| FR2711371B1 (fr) | 1993-10-18 | 1995-12-29 | Aetsrn | Procédé de préparation d'un concentré d'inter-alpha-trypsine inhibiteur à usage thérapeutique et concentré obtenu. |
| US5610285A (en) | 1994-08-24 | 1997-03-11 | Bayer Corporation | Purification of α-1 proteinase inhibitor using novel chromatographic separation conditions |
| DE4435485C1 (de) | 1994-10-04 | 1996-03-21 | Immuno Ag | Verfahren zur Gewinnung von hochreinem von Willebrand-Faktor |
| AUPN858596A0 (en) | 1996-03-08 | 1996-04-04 | Csl Limited | Filtration of plasma precipitates using cellulose filter aid |
| TW491855B (en) | 1996-08-07 | 2002-06-21 | Csl Ltd | Purification of immunoglobulins |
| US5783640A (en) * | 1997-03-04 | 1998-07-21 | The Goodyear Tire & Rubber Company | Rubber compositions containing a disodium salt of 2, 2'-dithiosalicyclic acid |
| CA2232420A1 (en) | 1997-03-19 | 1998-09-19 | The Green Cross Corporation | Immunoglobulin preparation and preparation process thereof |
| GB9705810D0 (en) | 1997-03-20 | 1997-05-07 | Common Services Agency | Intravenous immune globulin |
| AT407114B (de) | 1997-06-10 | 2000-12-27 | Immuno Ag | Alpha 1-antitrypsin-präparation sowie verfahren zu deren herstellung |
| US5886154A (en) * | 1997-06-20 | 1999-03-23 | Lebing; Wytold R. | Chromatographic method for high yield purification and viral inactivation of antibodies |
| PT911037E (pt) | 1997-10-23 | 2002-12-31 | Mitsubishi Pharma Corp | Preparacao de imunoglobulina armazenavel a temperatura ambiente para injeccao intravenosa |
| US20020114802A1 (en) | 1998-02-10 | 2002-08-22 | Tjellstrom Bo Arthur Einar | Oral immunoglobulin treatment for inflammatory bowel disease |
| AT406873B (de) | 1998-02-25 | 2000-10-25 | Immuno Ag | Verfahren zur abreicherung von pathogenen aus proteinhaltigen lösungen |
| DE19932782A1 (de) * | 1999-07-14 | 2001-01-18 | Biotest Pharma Gmbh | Verfahren zur chromatographischen Fraktionierung von Plasma oder Serum, so erhaltene Präparate und deren Verwendung |
| US6413245B1 (en) | 1999-10-21 | 2002-07-02 | Alcon Universal Ltd. | Sub-tenon drug delivery |
| DE10008519C1 (de) | 2000-02-21 | 2001-07-12 | Dica Technologies Ag | Verfahren und Kommunikationseinrichtungen zum Aufbau von gesicherten E-Mail-Verkehr zwischen Mail-Domains des Internet |
| DE10008619A1 (de) * | 2000-02-24 | 2001-09-06 | Immuno Vet As Lynge | Mikroorganismenfreies IgG-Präparat, Verfahren zu seiner Herstellung und seine Verwendung in der Tieraufzucht und in der Tiermast |
| SE0001128D0 (sv) | 2000-03-30 | 2000-03-30 | Amersham Pharm Biotech Ab | A method of producing IgG |
| US20020098182A1 (en) | 2000-09-28 | 2002-07-25 | Richard Weisbart | Treatment of immune-mediated diseases by oral administration of plasma fractions enriched in immunoglobulin G |
| WO2002030983A2 (de) | 2000-10-13 | 2002-04-18 | Octapharma Ag | Bikunin enthaltende plasmafraktion, verfahren zu ihrer herstellung und ihrer verwendung |
| FR2824568B1 (fr) | 2001-05-11 | 2004-04-09 | Lab Francais Du Fractionnement | Procede de preparation de concentres d'immunoglobulines humaines a usage therapeutique |
| WO2003028668A2 (en) | 2001-10-04 | 2003-04-10 | Protein Therapeutics, Inc. | Gammaglobulin treatment of immune disorders |
| US6893639B2 (en) | 2001-10-19 | 2005-05-17 | Hemacare Corporation | Method for high yield purification of immune globulins from blood plasma and blood plasma intermediates |
| US7777006B2 (en) | 2002-12-31 | 2010-08-17 | Csl Behring L.L.C. | Method for purification of alpha-1-antitrypsin |
| CN1780638B (zh) * | 2003-05-23 | 2010-04-14 | 诺和诺德医疗保健公司 | 氧化硅涂层玻璃作为容器内壁材料的用途及以该材料作内壁的容器 |
| WO2005012354A1 (en) | 2003-07-31 | 2005-02-10 | Zlb Behring Gmbh | Method for extending the half-life of fviii |
| US20050054003A1 (en) | 2003-09-10 | 2005-03-10 | Stenland Christopher J. | Prion clearance using particulate metal oxides |
| AU2004289252C1 (en) | 2003-11-08 | 2013-06-20 | Prothera Biologics, Inc. | Preparation and composition of Inter-alpha inhibitor proteins from human plasma for therapeutic use |
| EP1709077A1 (en) | 2004-01-30 | 2006-10-11 | Suomen Punainen Risti Veripalvelu | Process for the manufacture of virus safe immunoglobulin |
| PL1718675T3 (pl) | 2004-02-27 | 2013-09-30 | Octapharma Ag | Sposób uzyskiwania oczyszczonego preparatu przeciwciał pozbawionego wirusów |
| EP2357257B1 (en) | 2005-02-14 | 2019-07-31 | University of Iowa Research Foundation | Methods and reagents for treatment and diagnosis of age-related macular degeneration |
| US8715649B2 (en) | 2005-06-07 | 2014-05-06 | The Regents Of The University Of Colorado, A Body Corporate | Compositions and methods of use for alpha-1 antitrypsin having no significant serine protease inhibitor activity |
| US7807435B2 (en) | 2005-08-11 | 2010-10-05 | Baxter International Inc. | Method for the purification of alpha-1 proteinase inhibitor (a1PI) |
| WO2007038995A1 (en) | 2005-09-19 | 2007-04-12 | Csl Behring Gmbh | Factor h for the treatment of chronic nephropathies and production thereof |
| FR2894145B1 (fr) | 2005-12-07 | 2008-10-17 | Lab Francais Du Fractionnement | Utilisation de facteur h du complement a titre de medicament |
| EP1987054A1 (en) | 2006-01-25 | 2008-11-05 | Octapharma AG | Purification and use of a factor for supporting wound healing |
| US8476234B2 (en) | 2006-02-03 | 2013-07-02 | Prolor Biotech Inc. | Long-acting coagulation factors and methods of producing same |
| EP1852443A1 (en) * | 2006-05-05 | 2007-11-07 | Leukocare AG | Biocompatible three dimensional matrix for the immobilization of biological substances |
| DE102007001521A1 (de) * | 2007-01-10 | 2008-07-17 | Matthias, Torsten, Dr. | Verwendung von Cohn-Oncley-Fraktionen II und II/III zur Behandlung des systemischen Lupus erythematodes |
| WO2008113589A1 (en) | 2007-03-20 | 2008-09-25 | Csl Behring Gmbh | Methods for industrial scale production of therapeutic complement factor h preparations from human plasma |
| DE202007004346U1 (de) | 2007-03-21 | 2007-10-31 | Rehau Ag + Co | Rohranordnung |
| JP2010524971A (ja) * | 2007-04-20 | 2010-07-22 | ザ・リージェンツ・オブ・ザ・ユニバーシティ・オブ・コロラド，ア・ボディー・コーポレイト | 顕著なセリンプロテアーゼ阻害剤活性を有さないアルファ−１アンチトリプシン |
| JP2010529155A (ja) | 2007-06-13 | 2010-08-26 | ツェー・エス・エル・ベーリング・ゲー・エム・ベー・ハー | 出血性疾患の治療及び予防的処置における血管外投与のためのｖｗｆ安定化ｆｖｉｉｉ製剤及びｆｖｉｉｉなしのｖｗｆ製剤の使用 |
| EP2522753B1 (en) | 2007-08-13 | 2014-04-02 | Baxter International Inc. | IVIG modulation of chemokines for treatment of Multiple Sclerosis, Alzheimer's disease, and Parkinson's disease |
| CA2696417A1 (en) * | 2007-10-02 | 2009-04-09 | Csl Limited | Therapeutic antibody purification method and method of use |
| NZ586383A (en) | 2007-12-28 | 2012-11-30 | Baxter Int | Recombinant vwf formulations |
| CN101249265B (zh) * | 2008-04-11 | 2010-10-27 | 三九集团湛江开发区双林药业有限公司 | 静脉注射用人乙肝免疫球蛋白及其制备方法 |
| AU2009260822B2 (en) | 2008-05-28 | 2016-09-22 | Prothera Biologics, Inc. | Preparation and composition of Inter-alpha inhibitor proteins from blood |
| CN103739712B (zh) | 2008-06-24 | 2016-10-05 | 德国杰特贝林生物制品有限公司 | 具有延长的体内半衰期的因子viii、冯·维勒布兰德因子或它们的复合物 |
| CN201169579Y (zh) * | 2008-06-30 | 2008-12-24 | 山东泰邦生物制品有限公司 | 一种人血白蛋白分离用乙醇雾化扩散装置 |
| TWI670072B (zh) | 2008-10-21 | 2019-09-01 | 美商巴克斯歐塔公司 | 凍乾的重組ｖｗｆ調配物 |
| WO2010056909A1 (en) | 2008-11-12 | 2010-05-20 | Baxter International Inc. | Purification of butyrylcholinesterase using membrane adsorption |
| BRPI1012082B1 (pt) | 2009-05-27 | 2022-08-16 | Takeda Pharmaceutical Company Limited | Método para preparar uma composição de igg concentrada a partir de plasma |
| AT514675B1 (de) | 2009-07-23 | 2019-05-15 | Baxalta Inc | Herstellung von faktor h (fh) und fh-derivaten aus plasma |
| WO2011150284A2 (en) * | 2010-05-26 | 2011-12-01 | Baxter International Inc. | Removal of serine proteases by treatment with finely divided silicon dioxide |
| AU2010202125B1 (en) | 2010-05-26 | 2010-09-02 | Takeda Pharmaceutical Company Limited | A method to produce an immunoglobulin preparation with improved yield |
| ES3037386T3 (en) | 2010-07-08 | 2025-10-01 | Takeda Pharmaceuticals Co | Method of producing recombinant high molecular weight vwf in cell culture |
| US8841248B2 (en) | 2010-07-23 | 2014-09-23 | Baxter International Inc. | Manufacture of inter-alpha-inhibitor (IaIp) from plasma |
-
2010
- 2010-05-26 AU AU2010202125A patent/AU2010202125B1/en active Active
- 2010-05-27 CN CN201510158213.1A patent/CN104958761B/zh active Active
- 2010-05-27 KR KR1020167002347A patent/KR101647617B1/ko active Active
- 2010-05-27 BR BR112012029893-3A patent/BR112012029893B1/pt active IP Right Grant
- 2010-05-27 MY MYPI2012005077A patent/MY160551A/en unknown
- 2010-05-27 ES ES14176511T patent/ES2959234T3/es active Active
- 2010-05-27 US US12/789,365 patent/US8993734B2/en active Active
- 2010-05-27 EP EP14176511.5A patent/EP2803349B1/en active Active
- 2010-05-27 PL PL10727539T patent/PL2445482T3/pl unknown
- 2010-05-27 PT PT107275398T patent/PT2445482E/pt unknown
- 2010-05-27 EA EA201291355A patent/EA023446B1/ru not_active IP Right Cessation
- 2010-05-27 ES ES10727539.8T patent/ES2525492T3/es active Active
- 2010-05-27 DK DK12190138T patent/DK2554160T3/da active
- 2010-05-27 PL PL14176511.5T patent/PL2803349T3/pl unknown
- 2010-05-27 HR HRP20141109AT patent/HRP20141109T1/hr unknown
- 2010-05-27 CA CA2800155A patent/CA2800155A1/en not_active Abandoned
- 2010-05-27 PL PL12190138T patent/PL2554160T3/pl unknown
- 2010-05-27 EP EP12190138.3A patent/EP2554160B1/en active Active
- 2010-05-27 MX MX2014006981A patent/MX364252B/es unknown
- 2010-05-27 ES ES12190138.3T patent/ES2536093T3/es active Active
- 2010-05-27 SG SG2012086245A patent/SG185724A1/en unknown
- 2010-05-27 HU HUE14176511A patent/HUE064400T2/hu unknown
- 2010-05-27 CN CN201080067929.6A patent/CN102970975B/zh active Active
- 2010-05-27 KR KR1020127033758A patent/KR101593265B1/ko active Active
- 2010-05-27 MX MX2012013682A patent/MX349815B/es active IP Right Grant
- 2010-05-27 TW TW099117123A patent/TWI531577B/zh active
- 2010-05-27 MY MYPI2015002952A patent/MY173299A/en unknown
- 2010-05-27 AR ARP100101844A patent/AR076800A1/es active IP Right Grant
- 2010-05-27 JP JP2013512585A patent/JP5876474B2/ja active Active
- 2010-05-27 EA EA201500848A patent/EA034602B1/ru not_active IP Right Cessation
- 2010-05-27 EP EP10727539.8A patent/EP2445482B1/en active Active
- 2010-05-27 WO PCT/US2010/036470 patent/WO2011149472A1/en not_active Ceased
- 2010-05-27 SG SG10201505161SA patent/SG10201505161SA/en unknown
- 2010-05-27 DK DK10727539.8T patent/DK2445482T3/da active
- 2010-05-27 PT PT121901383T patent/PT2554160E/pt unknown
- 2010-09-29 AU AU2010224461A patent/AU2010224461B2/en active Active
-
2011
- 2011-05-26 KR KR1020127033759A patent/KR101716534B1/ko active Active
- 2011-05-26 CN CN201510171065.7A patent/CN104840946A/zh active Pending
- 2011-05-26 DK DK11729200.3T patent/DK2575762T3/da active
- 2011-05-26 TW TW104127086A patent/TWI543989B/zh active
- 2011-05-26 ES ES11729200.3T patent/ES2505465T3/es active Active
- 2011-05-26 CA CA2800272A patent/CA2800272A1/en not_active Abandoned
- 2011-05-26 AU AU2011258111A patent/AU2011258111B2/en active Active
- 2011-05-26 EP EP11729200.3A patent/EP2575762B1/en not_active Revoked
- 2011-05-26 SG SG2012086252A patent/SG185725A1/en unknown
- 2011-05-26 MY MYPI2012005078A patent/MY161617A/en unknown
- 2011-05-26 EA EA201691558A patent/EA034530B1/ru not_active IP Right Cessation
- 2011-05-26 EP EP20140166189 patent/EP2796128A1/en active Pending
- 2011-05-26 MX MX2012013689A patent/MX337028B/es active IP Right Grant
- 2011-05-26 BR BR112012029897A patent/BR112012029897A2/pt not_active Application Discontinuation
- 2011-05-26 EA EA201291367A patent/EA025826B1/ru not_active IP Right Cessation
- 2011-05-26 HR HRP20140944AT patent/HRP20140944T1/hr unknown
- 2011-05-26 PL PL11729200T patent/PL2575762T3/pl unknown
- 2011-05-26 EP EP22164436.2A patent/EP4039249A1/en active Pending
- 2011-05-26 CN CN201810967589.0A patent/CN109180776B/zh active Active
- 2011-05-26 AR ARP110101811A patent/AR082093A1/es active IP Right Grant
- 2011-05-26 PT PT117292003T patent/PT2575762E/pt unknown
- 2011-05-26 JP JP2013512262A patent/JP5866345B2/ja active Active
- 2011-05-26 CN CN201180036374.3A patent/CN103068365B/zh active Active
- 2011-05-26 TW TW100118581A patent/TWI504607B/zh active
-
2012
- 2012-10-16 US US13/653,332 patent/US8940877B2/en active Active
- 2012-11-20 IL IL223150A patent/IL223150A0/en unknown
- 2012-11-20 IL IL223149A patent/IL223149A/en active IP Right Grant
- 2012-11-23 CL CL2012003290A patent/CL2012003290A1/es unknown
- 2012-11-23 CO CO12212759A patent/CO6660439A2/es unknown
- 2012-11-23 CL CL2012003291A patent/CL2012003291A1/es unknown
- 2012-11-23 CO CO12212751A patent/CO6660438A2/es unknown
- 2012-11-26 MX MX2019004482A patent/MX2019004482A/es unknown
-
2014
- 2014-06-19 US US14/309,668 patent/US20150133644A1/en not_active Abandoned
- 2014-12-17 CL CL2014003430A patent/CL2014003430A1/es unknown
-
2015
- 2015-05-04 HR HRP20150484TT patent/HRP20150484T1/hr unknown
- 2015-08-14 JP JP2015160018A patent/JP2016053016A/ja active Pending
-
2016
- 2016-01-04 JP JP2016000025A patent/JP2016155798A/ja active Pending
- 2016-02-18 HK HK16101817.1A patent/HK1213790A1/zh unknown
- 2016-05-09 AU AU2016202973A patent/AU2016202973B2/en active Active
- 2016-10-27 JP JP2016210160A patent/JP6363676B2/ja active Active
-
2017
- 2017-11-08 US US15/807,512 patent/US11136350B2/en active Active
-
2018
- 2018-02-01 JP JP2018016073A patent/JP6592120B2/ja active Active
- 2018-02-26 AU AU2018201371A patent/AU2018201371B2/en active Active
-
2019
- 2019-01-23 AR ARP190100147A patent/AR114228A2/es unknown
-
2020
- 2020-01-19 AU AU2020200373A patent/AU2020200373B2/en active Active
-
2021
- 2021-04-16 AR ARP210101010A patent/AR121861A2/es unknown
- 2021-09-13 US US17/473,910 patent/US20210403504A1/en active Pending
- 2021-12-16 AU AU2021286395A patent/AU2021286395B2/en active Active
-
2023
- 2023-12-19 US US18/545,528 patent/US20240117009A1/en active Pending
-
2024
- 2024-07-11 AU AU2024204779A patent/AU2024204779A1/en active Pending
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US20210403504A1 (en) | Method to produce an immunoglobulin preparation with improved yield | |
| US8796430B2 (en) | Method to produce an immunoglobulin preparation with improved yield | |
| AU2024204995A1 (en) | A method to produce an immunoglobulin preparation with improved yield | |
| HK1181682B (en) | Method for preparing an enriched igg composition from plasma | |
| HK1203838B (en) | Method for preparing an enriched igg composition from plasma | |
| HK1170168B (en) | Method for preparing an enriched igg composition from plasma |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |
Effective date: 20160527 |