CA2254871C - Purification of biologically active peptides from milk - Google Patents
Purification of biologically active peptides from milk Download PDFInfo
- Publication number
- CA2254871C CA2254871C CA002254871A CA2254871A CA2254871C CA 2254871 C CA2254871 C CA 2254871C CA 002254871 A CA002254871 A CA 002254871A CA 2254871 A CA2254871 A CA 2254871A CA 2254871 C CA2254871 C CA 2254871C
- Authority
- CA
- Canada
- Prior art keywords
- milk
- protein
- capture device
- component
- permeate
- 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.)
- Expired - Lifetime
Links
- 210000004080 milk Anatomy 0.000 title claims abstract description 130
- 235000013336 milk Nutrition 0.000 title claims abstract description 126
- 239000008267 milk Substances 0.000 title claims abstract description 126
- 108090000765 processed proteins & peptides Proteins 0.000 title claims description 28
- 102000004196 processed proteins & peptides Human genes 0.000 title claims description 13
- 238000000746 purification Methods 0.000 title abstract description 20
- 238000000034 method Methods 0.000 claims abstract description 106
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 67
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 62
- 239000012466 permeate Substances 0.000 claims abstract description 52
- 238000009295 crossflow filtration Methods 0.000 claims abstract description 47
- 239000012465 retentate Substances 0.000 claims abstract description 35
- 239000012528 membrane Substances 0.000 claims abstract description 34
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims abstract description 32
- 230000009261 transgenic effect Effects 0.000 claims abstract description 25
- 239000002738 chelating agent Substances 0.000 claims abstract description 21
- 238000000605 extraction Methods 0.000 claims abstract description 15
- 235000018102 proteins Nutrition 0.000 claims description 59
- 102000004411 Antithrombin III Human genes 0.000 claims description 40
- 108090000935 Antithrombin III Proteins 0.000 claims description 40
- 229960005348 antithrombin iii Drugs 0.000 claims description 37
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 claims description 34
- 229960002897 heparin Drugs 0.000 claims description 34
- 229920000669 heparin Polymers 0.000 claims description 34
- 238000001914 filtration Methods 0.000 claims description 26
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 claims description 22
- 235000021240 caseins Nutrition 0.000 claims description 22
- 239000005018 casein Substances 0.000 claims description 20
- 241000700605 Viruses Species 0.000 claims description 19
- 238000001042 affinity chromatography Methods 0.000 claims description 18
- 238000004587 chromatography analysis Methods 0.000 claims description 18
- 239000000693 micelle Substances 0.000 claims description 16
- 238000011084 recovery Methods 0.000 claims description 15
- 210000001082 somatic cell Anatomy 0.000 claims description 15
- 102000014171 Milk Proteins Human genes 0.000 claims description 14
- 108010011756 Milk Proteins Proteins 0.000 claims description 14
- 235000021239 milk protein Nutrition 0.000 claims description 14
- 239000013618 particulate matter Substances 0.000 claims description 12
- 241000283707 Capra Species 0.000 claims description 10
- 239000011148 porous material Substances 0.000 claims description 10
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 claims description 9
- 241000124008 Mammalia Species 0.000 claims description 9
- 238000004255 ion exchange chromatography Methods 0.000 claims description 7
- 241000894006 Bacteria Species 0.000 claims description 6
- 108060003951 Immunoglobulin Proteins 0.000 claims description 6
- 108010063045 Lactoferrin Proteins 0.000 claims description 6
- 101710120037 Toxin CcdB Proteins 0.000 claims description 6
- 102000018358 immunoglobulin Human genes 0.000 claims description 6
- 229940078795 lactoferrin Drugs 0.000 claims description 6
- 102000010445 Lactoferrin Human genes 0.000 claims description 5
- 241000204031 Mycoplasma Species 0.000 claims description 5
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 claims description 5
- 235000021242 lactoferrin Nutrition 0.000 claims description 5
- 102000012286 Chitinases Human genes 0.000 claims description 4
- 108010022172 Chitinases Proteins 0.000 claims description 4
- 102000008192 Lactoglobulins Human genes 0.000 claims description 4
- 108010060630 Lactoglobulins Proteins 0.000 claims description 4
- DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 claims description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 claims description 4
- 102000004190 Enzymes Human genes 0.000 claims description 3
- 108090000790 Enzymes Proteins 0.000 claims description 3
- 102000004407 Lactalbumin Human genes 0.000 claims description 3
- 108090000942 Lactalbumin Proteins 0.000 claims description 3
- 241001494479 Pecora Species 0.000 claims description 3
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 claims description 3
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 claims description 3
- 229940088598 enzyme Drugs 0.000 claims description 3
- 229960004222 factor ix Drugs 0.000 claims description 3
- 239000003262 industrial enzyme Substances 0.000 claims description 3
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 claims description 3
- 235000020185 raw untreated milk Nutrition 0.000 claims description 3
- 108010043277 recombinant soluble CD4 Proteins 0.000 claims description 3
- 229960000187 tissue plasminogen activator Drugs 0.000 claims description 3
- KISWVXRQTGLFGD-UHFFFAOYSA-N 2-[[2-[[6-amino-2-[[2-[[2-[[5-amino-2-[[2-[[1-[2-[[6-amino-2-[(2,5-diamino-5-oxopentanoyl)amino]hexanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]-3-hydroxypropanoyl]amino]-5-oxopentanoyl]amino]-5-(diaminomethylideneamino)p Chemical compound C1CCN(C(=O)C(CCCN=C(N)N)NC(=O)C(CCCCN)NC(=O)C(N)CCC(N)=O)C1C(=O)NC(CO)C(=O)NC(CCC(N)=O)C(=O)NC(CCCN=C(N)N)C(=O)NC(CO)C(=O)NC(CCCCN)C(=O)NC(C(=O)NC(CC(C)C)C(O)=O)CC1=CC=C(O)C=C1 KISWVXRQTGLFGD-UHFFFAOYSA-N 0.000 claims description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 claims description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 claims description 2
- 102100022987 Angiogenin Human genes 0.000 claims description 2
- 102000004506 Blood Proteins Human genes 0.000 claims description 2
- 108010017384 Blood Proteins Proteins 0.000 claims description 2
- 241000283690 Bos taurus Species 0.000 claims description 2
- 102100022641 Coagulation factor IX Human genes 0.000 claims description 2
- 108090000394 Erythropoietin Proteins 0.000 claims description 2
- 108010076282 Factor IX Proteins 0.000 claims description 2
- 108010054218 Factor VIII Proteins 0.000 claims description 2
- 102000001690 Factor VIII Human genes 0.000 claims description 2
- 108010014173 Factor X Proteins 0.000 claims description 2
- 108010049003 Fibrinogen Proteins 0.000 claims description 2
- 102000008946 Fibrinogen Human genes 0.000 claims description 2
- 108010017544 Glucosylceramidase Proteins 0.000 claims description 2
- 102000004547 Glucosylceramidase Human genes 0.000 claims description 2
- 108091022930 Glutamate decarboxylase Proteins 0.000 claims description 2
- 102000008214 Glutamate decarboxylase Human genes 0.000 claims description 2
- 102000003886 Glycoproteins Human genes 0.000 claims description 2
- 108090000288 Glycoproteins Proteins 0.000 claims description 2
- 102000008100 Human Serum Albumin Human genes 0.000 claims description 2
- 108091006905 Human Serum Albumin Proteins 0.000 claims description 2
- 102100023915 Insulin Human genes 0.000 claims description 2
- 108090001061 Insulin Proteins 0.000 claims description 2
- 108010014251 Muramidase Proteins 0.000 claims description 2
- 241000699666 Mus <mouse, genus> Species 0.000 claims description 2
- 102000047918 Myelin Basic Human genes 0.000 claims description 2
- 101710107068 Myelin basic protein Proteins 0.000 claims description 2
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 claims description 2
- 102000029797 Prion Human genes 0.000 claims description 2
- 108091000054 Prion Proteins 0.000 claims description 2
- 108010076181 Proinsulin Proteins 0.000 claims description 2
- 241000700159 Rattus Species 0.000 claims description 2
- 102000019197 Superoxide Dismutase Human genes 0.000 claims description 2
- 108010012715 Superoxide dismutase Proteins 0.000 claims description 2
- 241000282898 Sus scrofa Species 0.000 claims description 2
- 102000015395 alpha 1-Antitrypsin Human genes 0.000 claims description 2
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 claims description 2
- 108010072788 angiogenin Proteins 0.000 claims description 2
- 230000001413 cellular effect Effects 0.000 claims description 2
- 229940105423 erythropoietin Drugs 0.000 claims description 2
- 229960000301 factor viii Drugs 0.000 claims description 2
- 229940012426 factor x Drugs 0.000 claims description 2
- 229940012952 fibrinogen Drugs 0.000 claims description 2
- 229940088597 hormone Drugs 0.000 claims description 2
- 239000005556 hormone Substances 0.000 claims description 2
- 229940072221 immunoglobulins Drugs 0.000 claims description 2
- 229940125396 insulin Drugs 0.000 claims description 2
- 235000010335 lysozyme Nutrition 0.000 claims description 2
- 229960000274 lysozyme Drugs 0.000 claims description 2
- 239000004325 lysozyme Substances 0.000 claims description 2
- 102000003951 Erythropoietin Human genes 0.000 claims 1
- 102000016943 Muramidase Human genes 0.000 claims 1
- 239000012569 microbial contaminant Substances 0.000 claims 1
- 239000002245 particle Substances 0.000 claims 1
- 239000000825 pharmaceutical preparation Substances 0.000 claims 1
- 108020003175 receptors Proteins 0.000 claims 1
- 241001465754 Metazoa Species 0.000 abstract description 19
- 230000001225 therapeutic effect Effects 0.000 abstract description 2
- 239000000523 sample Substances 0.000 description 24
- 230000008569 process Effects 0.000 description 22
- 238000000108 ultra-filtration Methods 0.000 description 20
- 235000008939 whole milk Nutrition 0.000 description 19
- 102000011632 Caseins Human genes 0.000 description 18
- 108010076119 Caseins Proteins 0.000 description 18
- 239000003925 fat Substances 0.000 description 18
- 239000000243 solution Substances 0.000 description 17
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 14
- 239000000872 buffer Substances 0.000 description 14
- 238000002955 isolation Methods 0.000 description 13
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 12
- 230000000694 effects Effects 0.000 description 11
- 210000004027 cell Anatomy 0.000 description 9
- 238000012545 processing Methods 0.000 description 9
- 239000001488 sodium phosphate Substances 0.000 description 9
- 229910000162 sodium phosphate Inorganic materials 0.000 description 9
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 9
- 108010046377 Whey Proteins Proteins 0.000 description 8
- 239000000047 product Substances 0.000 description 8
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- 108090000190 Thrombin Proteins 0.000 description 6
- 239000005862 Whey Substances 0.000 description 6
- 102000007544 Whey Proteins Human genes 0.000 description 6
- 230000004071 biological effect Effects 0.000 description 6
- 239000012510 hollow fiber Substances 0.000 description 6
- 150000002632 lipids Chemical class 0.000 description 6
- 229960004072 thrombin Drugs 0.000 description 6
- 238000003916 acid precipitation Methods 0.000 description 5
- 238000005119 centrifugation Methods 0.000 description 5
- 239000000356 contaminant Substances 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 238000003556 assay Methods 0.000 description 4
- 238000001556 precipitation Methods 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 230000009467 reduction Effects 0.000 description 4
- 235000020183 skimmed milk Nutrition 0.000 description 4
- 241000894007 species Species 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 3
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 241000701093 Suid alphaherpesvirus 1 Species 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 229910052791 calcium Inorganic materials 0.000 description 3
- 239000011575 calcium Substances 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 239000012501 chromatography medium Substances 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 3
- 235000013365 dairy product Nutrition 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 229950007919 egtazic acid Drugs 0.000 description 3
- 230000004907 flux Effects 0.000 description 3
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 239000001509 sodium citrate Substances 0.000 description 3
- 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 3
- 241001430294 unidentified retrovirus Species 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 2
- 241000991587 Enterovirus C Species 0.000 description 2
- 102100031939 Erythropoietin Human genes 0.000 description 2
- 241000274177 Juniperus sabina Species 0.000 description 2
- 241000701168 Murine adenovirus 1 Species 0.000 description 2
- 101000989950 Otolemur crassicaudatus Hemoglobin subunit alpha-A Proteins 0.000 description 2
- 238000011152 Q-Sepharose FF chromatography Methods 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 230000000996 additive effect Effects 0.000 description 2
- 150000001413 amino acids Chemical group 0.000 description 2
- 239000003114 blood coagulation factor Substances 0.000 description 2
- 229940021722 caseins Drugs 0.000 description 2
- 239000013522 chelant Substances 0.000 description 2
- 230000015271 coagulation Effects 0.000 description 2
- 238000005345 coagulation Methods 0.000 description 2
- 239000008367 deionised water Substances 0.000 description 2
- 229910021641 deionized water Inorganic materials 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 238000011026 diafiltration Methods 0.000 description 2
- 210000002919 epithelial cell Anatomy 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 238000005194 fractionation Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 235000021243 milk fat Nutrition 0.000 description 2
- 244000309711 non-enveloped viruses Species 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 230000002572 peristaltic effect Effects 0.000 description 2
- 230000006920 protein precipitation Effects 0.000 description 2
- 229940108461 rennet Drugs 0.000 description 2
- 108010058314 rennet Proteins 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- -1 somatic cells Substances 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 235000021119 whey protein Nutrition 0.000 description 2
- YDMBNDUHUNWWRP-VJBWXMMDSA-N (2s)-1-[(2r)-2-amino-3-phenylpropanoyl]-n-[(2s)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]piperidine-2-carboxamide Chemical compound C([C@@H](N)C(=O)N1[C@@H](CCCC1)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NC=1C=CC(=CC=1)[N+]([O-])=O)C1=CC=CC=C1 YDMBNDUHUNWWRP-VJBWXMMDSA-N 0.000 description 1
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 1
- 241000701242 Adenoviridae Species 0.000 description 1
- 108050000244 Alpha-s1 casein Proteins 0.000 description 1
- 101000766308 Bos taurus Serotransferrin Proteins 0.000 description 1
- 108090000746 Chymosin Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 102100026735 Coagulation factor VIII Human genes 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000700586 Herpesviridae Species 0.000 description 1
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 102000015335 Ku Autoantigen Human genes 0.000 description 1
- 108010025026 Ku Autoantigen Proteins 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 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
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 102100033468 Lysozyme C Human genes 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 241000709664 Picornaviridae Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 239000012564 Q sepharose fast flow resin Substances 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 241000712907 Retroviridae Species 0.000 description 1
- 241000282849 Ruminantia Species 0.000 description 1
- 108091006629 SLC13A2 Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 101000712605 Theromyzon tessulatum Theromin Proteins 0.000 description 1
- 229940122388 Thrombin inhibitor Drugs 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- 101710087237 Whey acidic protein Proteins 0.000 description 1
- 229960000583 acetic acid Drugs 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 108700010877 adenoviridae proteins Proteins 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000004019 antithrombin Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 1
- 235000008429 bread Nutrition 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 159000000007 calcium salts Chemical class 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 235000021277 colostrum Nutrition 0.000 description 1
- 210000003022 colostrum Anatomy 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 235000011850 desserts Nutrition 0.000 description 1
- 241001493065 dsRNA viruses Species 0.000 description 1
- 210000002969 egg yolk Anatomy 0.000 description 1
- 235000013345 egg yolk Nutrition 0.000 description 1
- 235000013601 eggs Nutrition 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000002270 exclusion chromatography Methods 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000013350 formula milk Nutrition 0.000 description 1
- 239000012362 glacial acetic acid Substances 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 235000020251 goat milk Nutrition 0.000 description 1
- 235000021244 human milk protein Nutrition 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 210000005075 mammary gland Anatomy 0.000 description 1
- 238000009285 membrane fouling Methods 0.000 description 1
- 229910044991 metal oxide Inorganic materials 0.000 description 1
- 239000012982 microporous membrane Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 238000000164 protein isolation Methods 0.000 description 1
- 238000011403 purification operation Methods 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 238000012421 spiking Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000012956 testing procedure Methods 0.000 description 1
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 239000003868 thrombin inhibitor Substances 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000013060 ultrafiltration and diafiltration Methods 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 210000003501 vero cell Anatomy 0.000 description 1
- 238000011100 viral filtration Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 238000003989 weak cation exchange chromatography Methods 0.000 description 1
- 235000021241 α-lactalbumin Nutrition 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J1/00—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites
- A23J1/20—Obtaining protein compositions for foodstuffs; Bulk opening of eggs and separation of yolks from whites from milk, e.g. casein; from whey
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/827—Proteins from mammals or birds
- Y10S530/832—Milk; colostrum
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biochemistry (AREA)
- Organic Chemistry (AREA)
- Biophysics (AREA)
- Medicinal Chemistry (AREA)
- Analytical Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Food Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Polymers & Plastics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/648,235 | 1996-05-13 | ||
| US08/648,235 US6268487B1 (en) | 1996-05-13 | 1996-05-13 | Purification of biologically active peptides from milk |
| PCT/US1997/008044 WO1997042835A1 (en) | 1996-05-13 | 1997-05-13 | Purification of biologically active peptides from milk |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2254871A1 CA2254871A1 (en) | 1997-11-20 |
| CA2254871C true CA2254871C (en) | 2008-03-25 |
Family
ID=24599969
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002254871A Expired - Lifetime CA2254871C (en) | 1996-05-13 | 1997-05-13 | Purification of biologically active peptides from milk |
Country Status (14)
| Country | Link |
|---|---|
| US (1) | US6268487B1 (cg-RX-API-DMAC7.html) |
| EP (1) | EP0923308B1 (cg-RX-API-DMAC7.html) |
| JP (1) | JP4476362B2 (cg-RX-API-DMAC7.html) |
| AT (1) | ATE224145T1 (cg-RX-API-DMAC7.html) |
| AU (1) | AU725993B2 (cg-RX-API-DMAC7.html) |
| CA (1) | CA2254871C (cg-RX-API-DMAC7.html) |
| DE (2) | DE69715641T2 (cg-RX-API-DMAC7.html) |
| DK (1) | DK0923308T3 (cg-RX-API-DMAC7.html) |
| ES (1) | ES2182074T3 (cg-RX-API-DMAC7.html) |
| LU (1) | LU91305I2 (cg-RX-API-DMAC7.html) |
| NL (1) | NL300256I2 (cg-RX-API-DMAC7.html) |
| NZ (1) | NZ332916A (cg-RX-API-DMAC7.html) |
| PT (1) | PT923308E (cg-RX-API-DMAC7.html) |
| WO (1) | WO1997042835A1 (cg-RX-API-DMAC7.html) |
Families Citing this family (71)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE122007000007I1 (de) | 1986-04-09 | 2007-05-16 | Genzyme Corp | Genetisch transformierte Tiere, die ein gewünschtes Protein in Milch absondern |
| CN1179048C (zh) | 1997-10-20 | 2004-12-08 | Gtc生物治疗学公司 | 修饰的MSP-1核酸序列以及增加细胞系统中mRNA水平和蛋白质表达的方法 |
| SE9802213D0 (sv) * | 1998-06-18 | 1998-06-18 | Amersham Pharm Biotech Ab | A method for the removal/purification of serum albumins and means for use in the method |
| US20030005468A1 (en) * | 1998-06-19 | 2003-01-02 | Meade Harry M. | Methods and vectors for improving nucleic acid expression |
| ATE328007T1 (de) * | 1998-09-24 | 2006-06-15 | Pharming Intellectual Pty Bv | Reinigung von fibrinogen aus flüssigkeiten mittels ausfällung und hydrophobischer- interaktion-chromatographie |
| CA2354638C (en) * | 1999-01-06 | 2013-03-19 | Atlantic Biopharmaceuticals, Inc. | Expression of secreted human alpha-fetoprotein in transgenic animals |
| WO2001000855A1 (en) | 1999-06-23 | 2001-01-04 | Ppl Therapeutics (Scotland) Ltd. | Fusion proteins incorporating lysozyme |
| AU5946501A (en) * | 2000-05-05 | 2001-11-20 | Genzyme Transgenics Corp | Transgenically produced decorin |
| US20020077775A1 (en) * | 2000-05-25 | 2002-06-20 | Schork Nicholas J. | Methods of DNA marker-based genetic analysis using estimated haplotype frequencies and uses thereof |
| US20030195707A1 (en) * | 2000-05-25 | 2003-10-16 | Schork Nicholas J | Methods of dna marker-based genetic analysis using estimated haplotype frequencies and uses thereof |
| US20040226052A1 (en) * | 2000-10-13 | 2004-11-11 | Meade Harry M. | Methods of producing a target molecule in a transgenic animal and purification of the target molecule |
| NZ529767A (en) * | 2001-06-13 | 2005-10-28 | Taurus Hsa Llc | Purification of human serum albumin |
| CA2456571A1 (en) * | 2001-08-10 | 2003-02-20 | Genset Sa | Human secreted proteins, their encoding polynucleotides, and uses thereof |
| US6875459B2 (en) * | 2001-09-10 | 2005-04-05 | Henry B. Kopf | Method and apparatus for separation of milk, colostrum, and whey |
| US20060253913A1 (en) * | 2001-12-21 | 2006-11-09 | Yue-Jin Huang | Production of hSA-linked butyrylcholinesterases in transgenic mammals |
| WO2003090545A1 (en) * | 2002-04-24 | 2003-11-06 | Dairy Development Specialists, Inc. | Intermediate ingredient for dairy product manufacturing and method of making the same |
| DE60227922D1 (de) * | 2002-05-27 | 2008-09-11 | Nestec Sa | Säurelösliche Proteine aus Casein-Micellen |
| GB0216001D0 (en) * | 2002-07-10 | 2002-08-21 | Nat Blood Authority | Process and composition |
| AU2003267135A1 (en) * | 2002-09-17 | 2004-04-08 | Gtc Biotherapeutics, Inc. | Isolation of immunoglobulin molecules that lack inter-heavy chain disulfide bonds |
| CA2506629A1 (en) * | 2002-11-27 | 2004-06-17 | Gtc Biotherapeutics, Inc. | Modified antibodies stably produced in milk and methods of producing same |
| US20040210953A1 (en) * | 2003-01-09 | 2004-10-21 | Murray James D. | Lysozyme transgenic ungulates |
| US20040231010A1 (en) * | 2003-01-09 | 2004-11-18 | Murray James D. | Lysozyme transgenic ungulates |
| ES2371913T3 (es) | 2003-01-22 | 2012-01-11 | Duke University | Constructos mejorados para expresar polipéptidos lisosomales. |
| US20040167320A1 (en) * | 2003-02-24 | 2004-08-26 | Couto Daniel E. | Methods of tangential flow filtration and an apparatus therefore |
| WO2005085287A1 (en) | 2004-03-03 | 2005-09-15 | En-N-Tech, Inc. | Treatments for contaminant reduction in lactoferrin preparations and lactoferrin-containing compositions |
| US20050197496A1 (en) * | 2004-03-04 | 2005-09-08 | Gtc Biotherapeutics, Inc. | Methods of protein fractionation using high performance tangential flow filtration |
| US20050245444A1 (en) * | 2004-04-30 | 2005-11-03 | Yann Echelard | Method of using recombinant human antithrombin for neurocognitive disorders |
| US20060121004A1 (en) * | 2004-12-07 | 2006-06-08 | Yann Echelard | Methods of reducing the incidence of rejection in tissue transplantation through the use of recombinant human antithrombin |
| US20060130159A1 (en) * | 2004-12-09 | 2006-06-15 | Nick Masiello | Method of purifying recombinant MSP 1-42 derived from Plasmodium falciparum |
| US20080019905A9 (en) * | 2005-02-18 | 2008-01-24 | Strome Scott E | Method of using an anti-CD137 antibody as an agent for radioimmunotherapy or radioimmunodetection |
| WO2006138647A2 (en) * | 2005-06-16 | 2006-12-28 | Gtc Biotherapeutics, Inc. | Method of making recombinant human antibodies for use in biosensor technology |
| US20070037192A1 (en) * | 2005-07-25 | 2007-02-15 | Gtc Biotherapeutics, Inc. | Method of purifying recombinant human antithrombin to enhance the viral and prion safety profile |
| CN101484470B (zh) * | 2005-10-21 | 2014-07-23 | 阿伊沃生物制剂有限公司 | 具有增强的抗体依赖性细胞毒性活性的抗体及其生产方法和用途 |
| US7531632B2 (en) * | 2006-02-16 | 2009-05-12 | Gtc Biotherapeutics, Inc. | Clarification of transgenic milk using depth filtration |
| FR2901707B1 (fr) | 2006-05-31 | 2017-09-29 | Lab Francais Du Fractionnement | Composition de facteur vii recombinant ou transgenique, chaque molecule de facteur vii possedant deux sites de n-glycosylation a motifs glycanniques definis |
| CA2659809A1 (en) * | 2006-08-04 | 2008-02-14 | Pharmathene Inc. | Long half-life recombinant butyrylcholinesterase |
| FR2910786B1 (fr) * | 2006-12-29 | 2017-08-11 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies (Lfb) | "procede d'extraction d'une proteine presente dans du lait" |
| JP5208428B2 (ja) * | 2007-01-30 | 2013-06-12 | 雪印メグミルク株式会社 | 美肌剤 |
| FR2912310B1 (fr) | 2007-02-13 | 2009-08-07 | Kasan Sarl | Nouvelles compositions cosmetiques et/ou pharmaceutiques et leurs applications. |
| ES2518290T3 (es) | 2007-07-10 | 2014-11-04 | Glanbia Nutritionals (Ireland) Limited | Método de eliminación de endotoxinas de proteínas |
| TWI346666B (en) * | 2007-12-31 | 2011-08-11 | Animal Technology Inst Taiwan | Method for seperating casein from casein-contained solution |
| EP2077273B1 (en) | 2007-12-31 | 2011-09-14 | Animal Technology Institute Taiwan | Methods for separating casein from soluble proteins in a composition |
| US8304005B2 (en) * | 2008-04-21 | 2012-11-06 | Fuji Oil Company, Limited | Method for production of defatted soymilk peptide |
| EP2279003A4 (en) * | 2008-05-01 | 2013-04-03 | Gtc Biotherapeutics Inc | ANTI-CD137 ANTIBODY AS A MEANS FOR THE TREATMENT OF INFLAMMATORY DISEASES |
| BRPI0911957A2 (pt) * | 2008-05-14 | 2016-08-23 | Agriculture Victoria Serv Pty | frações de leite enriquecidas com angiogenina |
| EP4328305A3 (en) * | 2009-12-18 | 2024-08-14 | CSL Ltd. | Method of purifying polypeptides |
| AU2010340358B2 (en) | 2009-12-21 | 2014-07-24 | Pharmathene, Inc. | Recombinant butyrylcholinesterases and truncates thereof |
| US8861162B2 (en) * | 2010-03-09 | 2014-10-14 | Honeywell International Inc. | High power solid state power controller (SSPC) solution for primary power distribution applications |
| FR2958496A1 (fr) * | 2010-04-09 | 2011-10-14 | Bioprotein Technologies Sa | Preparation de proteine plasmatique de transfert des phospholipides (pltp) humaine recombinante a partir du lait d'animaux transgeniques. |
| CN104959052B (zh) | 2010-04-09 | 2018-07-13 | 帕西拉制药有限公司 | 用于配制大直径合成膜囊泡的方法 |
| US10138290B2 (en) | 2010-10-05 | 2018-11-27 | Novo Nordisk Healthcare Ag | Process for protein production |
| CN103429272A (zh) | 2010-12-30 | 2013-12-04 | 法国化学与生物科技实验室 | 作为病原体灭活剂的二元醇 |
| US11154821B2 (en) | 2011-04-01 | 2021-10-26 | Emd Millipore Corporation | Nanofiber containing composite membrane structures |
| AU2012278836B2 (en) * | 2011-07-07 | 2016-03-10 | Lfb Usa, Inc. | Formulations that stabilize proteins |
| TW201400499A (zh) | 2012-03-12 | 2014-01-01 | Revo Biolog Inc | 抗凝血酶用於治療妊娠毒血症之用途 |
| EP2687595B1 (en) | 2012-07-19 | 2018-05-30 | Laboratoire Français du Fractionnement et des Biotechnologies | Method for purifying transgenic factor VII |
| WO2014022748A1 (en) | 2012-08-03 | 2014-02-06 | Revo Biologics, Inc. | The use of antithrombin in extracorporeal membrane oxygenation |
| KR20160002713A (ko) | 2013-02-13 | 2016-01-08 | 라보라토이레 프란카이즈 듀 프락티온네먼트 에트 데스 바이오테크놀로지스 | 고도로 갈락토실화된 항-tnf-알파 항체 및 이의 용도 |
| CN105263319A (zh) | 2013-02-13 | 2016-01-20 | 法国化学与生物科技实验室 | 具有经修饰的糖基化的蛋白及其生产方法 |
| MX384222B (es) | 2013-07-05 | 2025-03-14 | Lab Francais Du Fractionnement | Matriz de cromatografia de afinidad. |
| US9661868B2 (en) * | 2013-07-16 | 2017-05-30 | Mead Johnson Nutrition Company | Expanded bed adsorption methods for isolation of basic milk proteins including lactoferrin |
| AR100716A1 (es) * | 2014-06-02 | 2016-10-26 | Laboratoire Français Du Fractionnement Et Des Biotechnologies | Producción de fragmentos fc |
| SG11201608399QA (en) | 2014-06-26 | 2016-11-29 | Emd Millipore Corp | Filter structure with enhanced dirt holding capacity |
| FR3034419B1 (fr) | 2015-04-02 | 2017-12-15 | Lab Francais Du Fractionnement | Procede de purification d'une proteine recombinante therapeutique a partir d'un lait transgenique |
| KR102206959B1 (ko) | 2015-04-17 | 2021-01-25 | 이엠디 밀리포어 코포레이션 | 접선방향 유동 여과 모드에서 작동되는 나노섬유 한외여과막을 사용하여 샘플에서 목적하는 생물학적 물질을 정제하는 방법 |
| FR3038517B1 (fr) | 2015-07-06 | 2020-02-28 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Utilisation de fragments fc modifies en immunotherapie |
| EP3655142A1 (en) | 2017-07-21 | 2020-05-27 | Merck Millipore Ltd | Non-woven fiber membranes |
| CA3100869A1 (en) * | 2018-05-24 | 2019-11-28 | Jiangsu Hengrui Medicine Co., Ltd. | Method for preparing precursor of recombinant human insulin or analogue thereof |
| FR3082427B1 (fr) | 2018-06-14 | 2020-09-25 | Lab Francais Du Fractionnement | Combinaison de facteur vii et d'un anticorps bispecifique anti-facteurs ix et x |
| JP7478333B2 (ja) * | 2020-07-29 | 2024-05-07 | 和弘 原 | 成分調整物生産装置及び成分調整物生産方法 |
| CN113101737B (zh) * | 2021-03-04 | 2023-09-15 | 京美生命科技(杭州)有限公司 | 一种亲和切向流过滤系统及其构建方法和外泌体提取方法及应用 |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2459619B1 (fr) | 1979-06-26 | 1983-07-29 | Agronomique Inst Nat Rech | Procede pour l'obtention a partir de lactoserum, d'un produit enrichi en alpha-lactalbumine et applications dudit procede |
| FR2487642B2 (fr) | 1980-07-31 | 1985-10-18 | Bel Fromageries | Procede de preparation de fractions proteiques par ultrafiltration et chromatographie d'exclusion et d'echange d'ions |
| DE3432718C1 (de) | 1984-09-06 | 1986-05-22 | Biotest Pharma GmbH, 6000 Frankfurt | Verfahren zur Herstellung einer Loesung von Milch- und/oder Kolostralimmunglobulinen |
| FR2584727B1 (fr) | 1985-07-11 | 1988-06-17 | Roussel Uclaf | Procede d'extraction de proteines du lait, produits, application du procede, et compositions pharmaceutiques |
| JPS62298536A (ja) | 1986-06-17 | 1987-12-25 | Green Cross Corp:The | 生理活性物質の自動精製方法および自動精製装置 |
| DE3743440A1 (de) * | 1987-12-21 | 1989-06-29 | Gauri Kailash Kumar | Verfahren zum trennen der geloesten und ungeloesten bestandteile von milch |
| US4897465A (en) | 1988-10-12 | 1990-01-30 | Abbott Laboratories | Enrichment and concentration of proteins by ultrafiltration |
| MC2211A1 (fr) | 1989-12-01 | 1992-11-26 | Genpharm Int | Production de polypeptides recombinants par une espece bovine et procedes transgeniques |
| NL9001650A (nl) | 1990-07-19 | 1992-02-17 | Ver Coop Melkind | Werkwijze voor de bereiding van een melkeiwit-isolaat. |
| US5256294A (en) * | 1990-09-17 | 1993-10-26 | Genentech, Inc. | Tangential flow filtration process and apparatus |
| US5175013A (en) | 1990-12-31 | 1992-12-29 | The Pillsbury Company | Frozen dessert compositions and products |
| US5178894A (en) | 1991-09-26 | 1993-01-12 | Silvia P. Rudel | High non-fat milk content bread products having improved keeping qualities |
| EP0652889A4 (en) | 1992-06-15 | 1997-05-07 | Gene Pharming Europ Bv | PRODUCTION OF RECOMBINANT POLYPEPTIDES BY BOVINE SPECIES AND TRANSGENIC PROCESSES. |
| US5256437A (en) * | 1992-06-19 | 1993-10-26 | Pall Corporation | Product and process of making sterile milk through dynamic microfiltration |
| ES2146648T3 (es) | 1993-03-09 | 2000-08-16 | Genzyme Corp | Procedimiento de aislamiento de proteinas de la leche. |
| AU1809895A (en) | 1994-02-16 | 1995-09-04 | Pharming Bv | Isolation of lactoferrin from milk |
| US5597486A (en) * | 1995-05-01 | 1997-01-28 | Millipore Investment Holdings Limited | Membrane filtration with optimized addition of second liquid to maximize flux |
-
1996
- 1996-05-13 US US08/648,235 patent/US6268487B1/en not_active Expired - Lifetime
-
1997
- 1997-05-13 WO PCT/US1997/008044 patent/WO1997042835A1/en not_active Ceased
- 1997-05-13 DK DK97923643T patent/DK0923308T3/da active
- 1997-05-13 NZ NZ332916A patent/NZ332916A/xx not_active IP Right Cessation
- 1997-05-13 ES ES97923643T patent/ES2182074T3/es not_active Expired - Lifetime
- 1997-05-13 DE DE69715641T patent/DE69715641T2/de not_active Expired - Lifetime
- 1997-05-13 DE DE122007000008C patent/DE122007000008I2/de active Active
- 1997-05-13 JP JP54103697A patent/JP4476362B2/ja not_active Expired - Lifetime
- 1997-05-13 CA CA002254871A patent/CA2254871C/en not_active Expired - Lifetime
- 1997-05-13 EP EP97923643A patent/EP0923308B1/en not_active Expired - Lifetime
- 1997-05-13 PT PT97923643T patent/PT923308E/pt unknown
- 1997-05-13 AT AT97923643T patent/ATE224145T1/de active
- 1997-05-13 AU AU29402/97A patent/AU725993B2/en not_active Expired
-
2007
- 2007-01-12 LU LU91305C patent/LU91305I2/fr unknown
- 2007-01-19 NL NL300256C patent/NL300256I2/nl unknown
Also Published As
| Publication number | Publication date |
|---|---|
| NL300256I2 (nl) | 2007-09-03 |
| DE122007000008I2 (de) | 2011-01-13 |
| NZ332916A (en) | 2000-05-26 |
| DE122007000008I1 (de) | 2009-05-20 |
| DK0923308T3 (da) | 2002-10-14 |
| AU2940297A (en) | 1997-12-05 |
| JP4476362B2 (ja) | 2010-06-09 |
| DE69715641T2 (de) | 2003-08-07 |
| ATE224145T1 (de) | 2002-10-15 |
| JP2000510701A (ja) | 2000-08-22 |
| NL300256I1 (nl) | 2007-04-02 |
| ES2182074T3 (es) | 2003-03-01 |
| WO1997042835A1 (en) | 1997-11-20 |
| LU91305I2 (fr) | 2007-03-12 |
| EP0923308A1 (en) | 1999-06-23 |
| AU725993B2 (en) | 2000-10-26 |
| EP0923308B1 (en) | 2002-09-18 |
| PT923308E (pt) | 2002-11-29 |
| EP0923308A4 (cg-RX-API-DMAC7.html) | 1999-06-30 |
| US6268487B1 (en) | 2001-07-31 |
| DE69715641D1 (de) | 2002-10-24 |
| CA2254871A1 (en) | 1997-11-20 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2254871C (en) | Purification of biologically active peptides from milk | |
| EP1991063B1 (en) | Clarification of transgenic milk using depth filtration | |
| CA2192683C (en) | Filtration | |
| JP3801196B2 (ja) | 乳からの対象化合物の単離 | |
| US20040167320A1 (en) | Methods of tangential flow filtration and an apparatus therefore | |
| US5500229A (en) | Colostrum fraction, a process of preparing it and its use as a supplement in cell culture media | |
| JP2007526302A (ja) | 高性能タンジェンシャルフローフィルトレーションを用いるタンパク質分画方法 | |
| US20030026845A1 (en) | Process for preparing protein isolate from milk, whey, colostrum, and the like | |
| NZ243727A (en) | Isolation of charged particles from fluids by ion exchange where the ion exchange medium is disposed on a porous membrane | |
| CA2157118C (en) | Isolation of components of interest from milk | |
| AU682274C (en) | Filtration | |
| AU2376292A (en) | Isolation of charged particles from fluids |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| MKEX | Expiry |
Effective date: 20170515 |