MXPA06000944A - Composiciones para purificar y cristalizar moleculas de interes. - Google Patents
Composiciones para purificar y cristalizar moleculas de interes.Info
- Publication number
- MXPA06000944A MXPA06000944A MXPA06000944A MXPA06000944A MXPA06000944A MX PA06000944 A MXPA06000944 A MX PA06000944A MX PA06000944 A MXPA06000944 A MX PA06000944A MX PA06000944 A MXPA06000944 A MX PA06000944A MX PA06000944 A MXPA06000944 A MX PA06000944A
- Authority
- MX
- Mexico
- Prior art keywords
- interest
- molecule
- ligand
- composition
- cell
- Prior art date
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 98
- 239000003446 ligand Substances 0.000 claims abstract description 147
- 238000000034 method Methods 0.000 claims abstract description 94
- 230000027455 binding Effects 0.000 claims abstract description 44
- 238000002425 crystallisation Methods 0.000 claims abstract description 30
- 230000008025 crystallization Effects 0.000 claims abstract description 28
- 102000004169 proteins and genes Human genes 0.000 claims description 65
- 108090000623 proteins and genes Proteins 0.000 claims description 65
- 210000004027 cell Anatomy 0.000 claims description 48
- 230000015572 biosynthetic process Effects 0.000 claims description 40
- 229920000642 polymer Polymers 0.000 claims description 35
- 239000002738 chelating agent Substances 0.000 claims description 34
- 150000002500 ions Chemical class 0.000 claims description 33
- 239000000523 sample Substances 0.000 claims description 33
- 239000013078 crystal Substances 0.000 claims description 28
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 claims description 18
- 239000002244 precipitate Substances 0.000 claims description 17
- 238000005304 joining Methods 0.000 claims description 12
- 150000007523 nucleic acids Chemical group 0.000 claims description 12
- 239000000126 substance Substances 0.000 claims description 12
- 229960002685 biotin Drugs 0.000 claims description 10
- 239000011616 biotin Substances 0.000 claims description 10
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 10
- 235000020958 biotin Nutrition 0.000 claims description 9
- 108090001008 Avidin Proteins 0.000 claims description 8
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 8
- 201000010099 disease Diseases 0.000 claims description 8
- 108090000790 Enzymes Proteins 0.000 claims description 7
- 102000004190 Enzymes Human genes 0.000 claims description 7
- 230000005847 immunogenicity Effects 0.000 claims description 7
- 239000012472 biological sample Substances 0.000 claims description 6
- 239000003102 growth factor Substances 0.000 claims description 5
- 230000006698 induction Effects 0.000 claims description 5
- 239000000758 substrate Substances 0.000 claims description 5
- 229910021645 metal ion Inorganic materials 0.000 claims description 4
- 150000003384 small molecules Chemical class 0.000 claims description 4
- 230000003612 virological effect Effects 0.000 claims description 4
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 2
- 239000005556 hormone Substances 0.000 claims description 2
- 229940088597 hormone Drugs 0.000 claims description 2
- 210000001236 prokaryotic cell Anatomy 0.000 claims description 2
- 108020004707 nucleic acids Proteins 0.000 claims 1
- 102000039446 nucleic acids Human genes 0.000 claims 1
- 238000000746 purification Methods 0.000 abstract description 23
- 230000003053 immunization Effects 0.000 abstract 1
- 238000002649 immunization Methods 0.000 abstract 1
- 238000001556 precipitation Methods 0.000 description 24
- 239000002184 metal Substances 0.000 description 23
- 229910052751 metal Inorganic materials 0.000 description 23
- 108010052285 Membrane Proteins Proteins 0.000 description 16
- 108090000765 processed proteins & peptides Proteins 0.000 description 13
- 239000000243 solution Substances 0.000 description 11
- 238000003786 synthesis reaction Methods 0.000 description 11
- 239000003599 detergent Substances 0.000 description 10
- 238000010828 elution Methods 0.000 description 10
- 239000000427 antigen Substances 0.000 description 9
- 108091007433 antigens Proteins 0.000 description 9
- 102000036639 antigens Human genes 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 238000000787 affinity precipitation Methods 0.000 description 8
- 239000012535 impurity Substances 0.000 description 8
- 230000003993 interaction Effects 0.000 description 8
- 230000008569 process Effects 0.000 description 8
- 238000002955 isolation Methods 0.000 description 7
- 150000002739 metals Chemical class 0.000 description 7
- 102000004196 processed proteins & peptides Human genes 0.000 description 7
- 238000000926 separation method Methods 0.000 description 7
- SIKJAQJRHWYJAI-UHFFFAOYSA-N Indole Chemical compound C1=CC=C2NC=CC2=C1 SIKJAQJRHWYJAI-UHFFFAOYSA-N 0.000 description 6
- 230000008901 benefit Effects 0.000 description 6
- 239000011159 matrix material Substances 0.000 description 6
- 230000000890 antigenic effect Effects 0.000 description 5
- 239000000356 contaminant Substances 0.000 description 5
- 238000000502 dialysis Methods 0.000 description 5
- 238000012986 modification Methods 0.000 description 5
- 230000004048 modification Effects 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 239000013638 trimer Substances 0.000 description 5
- 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 description 4
- 102000018697 Membrane Proteins Human genes 0.000 description 4
- 238000001042 affinity chromatography Methods 0.000 description 4
- YCIMNLLNPGFGHC-UHFFFAOYSA-N catechol Chemical compound OC1=CC=CC=C1O YCIMNLLNPGFGHC-UHFFFAOYSA-N 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 230000012010 growth Effects 0.000 description 4
- 229920000669 heparin Polymers 0.000 description 4
- 229960002897 heparin Drugs 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 229920002521 macromolecule Polymers 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000002609 medium Substances 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 238000001742 protein purification Methods 0.000 description 4
- 230000008929 regeneration Effects 0.000 description 4
- 238000011069 regeneration method Methods 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 238000000108 ultra-filtration Methods 0.000 description 4
- 208000024827 Alzheimer disease Diseases 0.000 description 3
- 239000000370 acceptor Substances 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 238000011109 contamination Methods 0.000 description 3
- 238000009792 diffusion process Methods 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 230000002163 immunogen Effects 0.000 description 3
- PZOUSPYUWWUPPK-UHFFFAOYSA-N indole Natural products CC1=CC=CC2=C1C=CN2 PZOUSPYUWWUPPK-UHFFFAOYSA-N 0.000 description 3
- RKJUIXBNRJVNHR-UHFFFAOYSA-N indolenine Natural products C1=CC=C2CC=NC2=C1 RKJUIXBNRJVNHR-UHFFFAOYSA-N 0.000 description 3
- 150000002632 lipids Chemical class 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 238000011068 loading method Methods 0.000 description 3
- 230000033001 locomotion Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 210000000056 organ Anatomy 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 230000002194 synthesizing effect Effects 0.000 description 3
- 102000004506 Blood Proteins Human genes 0.000 description 2
- 108010017384 Blood Proteins Proteins 0.000 description 2
- 108010062580 Concanavalin A Proteins 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 206010067889 Dementia with Lewy bodies Diseases 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108090001090 Lectins Proteins 0.000 description 2
- 102000004856 Lectins Human genes 0.000 description 2
- 201000002832 Lewy body dementia Diseases 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 208000018737 Parkinson disease Diseases 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- 101710120037 Toxin CcdB Proteins 0.000 description 2
- UATJOMSPNYCXIX-UHFFFAOYSA-N Trinitrobenzene Chemical compound [O-][N+](=O)C1=CC([N+]([O-])=O)=CC([N+]([O-])=O)=C1 UATJOMSPNYCXIX-UHFFFAOYSA-N 0.000 description 2
- 238000002441 X-ray diffraction Methods 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000005875 antibody response Effects 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 235000013361 beverage Nutrition 0.000 description 2
- 238000002306 biochemical method Methods 0.000 description 2
- 210000001185 bone marrow Anatomy 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 150000001768 cations Chemical class 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 239000013522 chelant Substances 0.000 description 2
- 238000004132 cross linking Methods 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000011033 desalting Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 230000007613 environmental effect Effects 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 239000000017 hydrogel Substances 0.000 description 2
- NBZBKCUXIYYUSX-UHFFFAOYSA-N iminodiacetic acid Chemical compound OC(=O)CNCC(O)=O NBZBKCUXIYYUSX-UHFFFAOYSA-N 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 239000002523 lectin Substances 0.000 description 2
- 238000012423 maintenance Methods 0.000 description 2
- 239000000693 micelle Substances 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 238000005191 phase separation Methods 0.000 description 2
- OXNIZHLAWKMVMX-UHFFFAOYSA-N picric acid Chemical compound OC1=C([N+]([O-])=O)C=C([N+]([O-])=O)C=C1[N+]([O-])=O OXNIZHLAWKMVMX-UHFFFAOYSA-N 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 238000012514 protein characterization Methods 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 210000000130 stem cell Anatomy 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- PGAPPWIQQVLWKV-UHFFFAOYSA-N 1h-indole;2,4,6-trinitrophenol Chemical compound C1=CC=C2NC=CC2=C1.OC1=C([N+]([O-])=O)C=C([N+]([O-])=O)C=C1[N+]([O-])=O PGAPPWIQQVLWKV-UHFFFAOYSA-N 0.000 description 1
- JOERSAVCLPYNIZ-UHFFFAOYSA-N 2,4,5,7-tetranitrofluoren-9-one Chemical compound O=C1C2=CC([N+]([O-])=O)=CC([N+]([O-])=O)=C2C2=C1C=C([N+](=O)[O-])C=C2[N+]([O-])=O JOERSAVCLPYNIZ-UHFFFAOYSA-N 0.000 description 1
- IHDBZCJYSHDCKF-UHFFFAOYSA-N 4,6-dichlorotriazine Chemical compound ClC1=CC(Cl)=NN=N1 IHDBZCJYSHDCKF-UHFFFAOYSA-N 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 101710137189 Amyloid-beta A4 protein Proteins 0.000 description 1
- 101710151993 Amyloid-beta precursor protein Proteins 0.000 description 1
- 102100022704 Amyloid-beta precursor protein Human genes 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 101710081722 Antitrypsin Proteins 0.000 description 1
- 108091023037 Aptamer Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 102000000584 Calmodulin Human genes 0.000 description 1
- 108010041952 Calmodulin Proteins 0.000 description 1
- 102100026735 Coagulation factor VIII Human genes 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 201000003542 Factor VIII deficiency Diseases 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 102000014702 Haptoglobin Human genes 0.000 description 1
- 108050005077 Haptoglobin Proteins 0.000 description 1
- 102100031573 Hematopoietic progenitor cell antigen CD34 Human genes 0.000 description 1
- 208000009292 Hemophilia A Diseases 0.000 description 1
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 1
- 101000777663 Homo sapiens Hematopoietic progenitor cell antigen CD34 Proteins 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 235000010254 Jasminum officinale Nutrition 0.000 description 1
- 240000005385 Jasminum sambac Species 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 208000025966 Neurological disease Diseases 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 241000282320 Panthera leo Species 0.000 description 1
- 206010034016 Paronychia Diseases 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108091000054 Prion Proteins 0.000 description 1
- 102000029797 Prion Human genes 0.000 description 1
- 206010060862 Prostate cancer Diseases 0.000 description 1
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010026552 Proteome Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 108010034949 Thyroglobulin Proteins 0.000 description 1
- 102000009843 Thyroglobulin Human genes 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 208000027276 Von Willebrand disease Diseases 0.000 description 1
- DGEZNRSVGBDHLK-UHFFFAOYSA-N [1,10]phenanthroline Chemical compound C1=CN=C2C3=NC=CC=C3C=CC2=C1 DGEZNRSVGBDHLK-UHFFFAOYSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- PYKYMHQGRFAEBM-UHFFFAOYSA-N anthraquinone Natural products CCC(=O)c1c(O)c2C(=O)C3C(C=CC=C3O)C(=O)c2cc1CC(=O)OC PYKYMHQGRFAEBM-UHFFFAOYSA-N 0.000 description 1
- 150000004056 anthraquinones Chemical class 0.000 description 1
- 230000001475 anti-trypsic effect Effects 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000004429 atom Chemical group 0.000 description 1
- 239000000987 azo dye Substances 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 238000010170 biological method Methods 0.000 description 1
- 150000001615 biotins Chemical class 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 239000002771 cell marker Substances 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 238000012993 chemical processing Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000011098 chromatofocusing Methods 0.000 description 1
- 239000012539 chromatography resin Substances 0.000 description 1
- YKCWQPZFAFZLBI-UHFFFAOYSA-N cibacron blue Chemical compound C1=2C(=O)C3=CC=CC=C3C(=O)C=2C(N)=C(S(O)(=O)=O)C=C1NC(C=C1S(O)(=O)=O)=CC=C1NC(N=1)=NC(Cl)=NC=1NC1=CC=CC=C1S(O)(=O)=O YKCWQPZFAFZLBI-UHFFFAOYSA-N 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 230000009918 complex formation Effects 0.000 description 1
- 239000003636 conditioned culture medium Substances 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 239000000599 controlled substance Substances 0.000 description 1
- 239000007799 cork Substances 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 238000002651 drug therapy Methods 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 150000004820 halides Chemical class 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 1
- -1 heparin) Chemical class 0.000 description 1
- 125000000623 heterocyclic group Chemical group 0.000 description 1
- 239000012456 homogeneous solution Substances 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical class [H]* 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 101150026046 iga gene Proteins 0.000 description 1
- 210000001822 immobilized cell Anatomy 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 150000002475 indoles Chemical class 0.000 description 1
- 125000001041 indolyl group Chemical group 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 210000002751 lymph Anatomy 0.000 description 1
- 230000001926 lymphatic effect Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 239000005445 natural material Substances 0.000 description 1
- 229920005615 natural polymer Polymers 0.000 description 1
- 239000006225 natural substrate Substances 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 230000004770 neurodegeneration Effects 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 239000002547 new drug Substances 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- 239000013631 noncovalent dimer Substances 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 230000005305 organ development Effects 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 239000013636 protein dimer Substances 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000004850 protein–protein interaction Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 239000011535 reaction buffer Substances 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000009256 replacement therapy Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000241 respiratory effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 238000011012 sanitization Methods 0.000 description 1
- 239000012047 saturated solution Substances 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 238000007711 solidification Methods 0.000 description 1
- 230000008023 solidification Effects 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 230000007480 spreading Effects 0.000 description 1
- 238000003892 spreading Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- IXHMHWIBCIYOAZ-UHFFFAOYSA-N styphnic acid Chemical compound OC1=C([N+]([O-])=O)C=C([N+]([O-])=O)C(O)=C1[N+]([O-])=O IXHMHWIBCIYOAZ-UHFFFAOYSA-N 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 230000000946 synaptic effect Effects 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 210000001138 tear Anatomy 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 210000001541 thymus gland Anatomy 0.000 description 1
- 229960002175 thyroglobulin Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 150000005186 trinitrobenzenes Chemical class 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 108010047303 von Willebrand Factor Proteins 0.000 description 1
- 208000012137 von Willebrand disease (hereditary or acquired) Diseases 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07H—SUGARS; DERIVATIVES THEREOF; NUCLEOSIDES; NUCLEOTIDES; NUCLEIC ACIDS
- C07H21/00—Compounds containing two or more mononucleotide units having separate phosphate or polyphosphate groups linked by saccharide radicals of nucleoside groups, e.g. nucleic 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
- A61K47/50—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 the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—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 the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/54—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 the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic compound
- A61K47/555—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 the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic compound pre-targeting systems involving an organic compound, other than a peptide, protein or antibody, for targeting specific cells
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Medicinal Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Biomedical Technology (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Engineering & Computer Science (AREA)
- Immunology (AREA)
- Epidemiology (AREA)
- Biophysics (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Crystallography & Structural Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Plant Pathology (AREA)
- Microbiology (AREA)
- General Chemical & Material Sciences (AREA)
- Physics & Mathematics (AREA)
- Peptides Or Proteins (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Medicinal Preparation (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| IL15708603A IL157086A0 (en) | 2003-07-24 | 2003-07-24 | Multivalent ligand complexes |
| PCT/IL2004/000669 WO2005010141A2 (en) | 2003-07-24 | 2004-07-22 | Compositions for purifying and crystallizing molecules of interest |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MXPA06000944A true MXPA06000944A (es) | 2006-03-30 |
Family
ID=32652285
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MXPA06000944A MXPA06000944A (es) | 2003-07-24 | 2004-07-22 | Composiciones para purificar y cristalizar moleculas de interes. |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US20060121519A1 (https=) |
| EP (1) | EP1648995A4 (https=) |
| JP (1) | JP2007515384A (https=) |
| KR (1) | KR20060037337A (https=) |
| CN (1) | CN101415721A (https=) |
| CA (1) | CA2531492A1 (https=) |
| IL (2) | IL157086A0 (https=) |
| MX (1) | MXPA06000944A (https=) |
| NO (1) | NO20060400L (https=) |
| RU (1) | RU2006105648A (https=) |
| SG (1) | SG145760A1 (https=) |
| WO (1) | WO2005010141A2 (https=) |
| ZA (1) | ZA200600315B (https=) |
Families Citing this family (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7956165B2 (en) | 2003-07-24 | 2011-06-07 | Affisink Biotechnology Ltd. | Compositions and methods for purifying and crystallizing molecules of interest |
| WO2006085321A2 (en) * | 2005-02-10 | 2006-08-17 | Affisink Biotechnology Ltd. | Compositions and methods for purifying and crystallizing molecules of interest |
| FR2902799B1 (fr) | 2006-06-27 | 2012-10-26 | Millipore Corp | Procede et unite de preparation d'un echantillon pour l'analyse microbiologique d'un liquide |
| US8362217B2 (en) | 2006-12-21 | 2013-01-29 | Emd Millipore Corporation | Purification of proteins |
| WO2008079302A2 (en) * | 2006-12-21 | 2008-07-03 | Millipore Corporation | Purification of proteins |
| US8569464B2 (en) | 2006-12-21 | 2013-10-29 | Emd Millipore Corporation | Purification of proteins |
| US20100233714A1 (en) * | 2007-11-13 | 2010-09-16 | Beadling Leslie C | Multistate affinity ligands for the separation and purification of antibodies, antibody fragments and conjugates of |
| WO2009078018A2 (en) * | 2007-12-17 | 2009-06-25 | Affisink Biotechnology Ltd. | Methods for purifying or depleting molecules or cells of interest |
| US8999702B2 (en) | 2008-06-11 | 2015-04-07 | Emd Millipore Corporation | Stirred tank bioreactor |
| JP2012511929A (ja) | 2008-12-16 | 2012-05-31 | イー・エム・デイー・ミリポア・コーポレイシヨン | 攪拌タンク反応器及び方法 |
| CA2791918C (en) | 2010-03-05 | 2019-11-19 | Boehringer Ingelheim International Gmbh | Selective enrichment of antibodies |
| WO2011146394A1 (en) | 2010-05-17 | 2011-11-24 | Millipore Corporation | Stimulus responsive polymers for the purification of biomolecules |
| US10030224B2 (en) | 2015-11-01 | 2018-07-24 | Ariel-University Research And Development Company Ltd. | Methods of analyzing cell membranes |
| WO2021152584A1 (en) | 2020-01-28 | 2021-08-05 | Ariel Scientific Innovations Ltd. | Methods of analyzing cell membranes |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4036945A (en) * | 1976-05-03 | 1977-07-19 | The Massachusetts General Hospital | Composition and method for determining the size and location of myocardial infarcts |
| US4331647A (en) * | 1980-03-03 | 1982-05-25 | Goldenberg Milton David | Tumor localization and therapy with labeled antibody fragments specific to tumor-associated markers |
| US5215927A (en) * | 1986-01-30 | 1993-06-01 | Fred Hutchinson Cancer Research Center | Method for immunoselection of cells using avidin and biotin |
| US4946778A (en) * | 1987-09-21 | 1990-08-07 | Genex Corporation | Single polypeptide chain binding molecules |
| US6740734B1 (en) * | 1994-01-14 | 2004-05-25 | Biovitrum Ab | Bacterial receptor structures |
| SE9400088D0 (sv) * | 1994-01-14 | 1994-01-14 | Kabi Pharmacia Ab | Bacterial receptor structures |
| US6017719A (en) * | 1994-06-14 | 2000-01-25 | Nexell Therapeutics, Inc. | Positive and positive/negative cell selection mediated by peptide release |
| US20010008766A1 (en) * | 1998-03-17 | 2001-07-19 | Sylvia Daunert | Quantitative binding assays using green fluorescent protein as a label |
| US6589503B1 (en) * | 1998-06-20 | 2003-07-08 | Washington University | Membrane-permeant peptide complexes for medical imaging, diagnostics, and pharmaceutical therapy |
| US7198930B2 (en) * | 2000-02-29 | 2007-04-03 | Millennium Pharmaceuticals, Inc. | Human protein kinase, phosphatase, and protease family members and uses thereof |
| DE60231801D1 (de) * | 2001-04-23 | 2009-05-14 | Mallinckrodt Inc | Tc und re markierte radioaktive glycosylierte octreotid-derivate |
| US20040265921A1 (en) * | 2003-06-30 | 2004-12-30 | National University Of Singapore | Intein-mediated attachment of ligands to proteins for immobilization onto a support |
| US7956165B2 (en) * | 2003-07-24 | 2011-06-07 | Affisink Biotechnology Ltd. | Compositions and methods for purifying and crystallizing molecules of interest |
-
2003
- 2003-07-24 IL IL15708603A patent/IL157086A0/xx unknown
-
2004
- 2004-07-22 SG SG200806175-6A patent/SG145760A1/en unknown
- 2004-07-22 WO PCT/IL2004/000669 patent/WO2005010141A2/en not_active Ceased
- 2004-07-22 MX MXPA06000944A patent/MXPA06000944A/es not_active Application Discontinuation
- 2004-07-22 KR KR1020067000635A patent/KR20060037337A/ko not_active Withdrawn
- 2004-07-22 CA CA002531492A patent/CA2531492A1/en not_active Abandoned
- 2004-07-22 CN CNA2004800263533A patent/CN101415721A/zh active Pending
- 2004-07-22 RU RU2006105648/13A patent/RU2006105648A/ru not_active Application Discontinuation
- 2004-07-22 JP JP2006520982A patent/JP2007515384A/ja active Pending
- 2004-07-22 EP EP04745009A patent/EP1648995A4/en not_active Withdrawn
-
2006
- 2006-01-12 IL IL173107A patent/IL173107A0/en unknown
- 2006-01-12 ZA ZA200600315A patent/ZA200600315B/xx unknown
- 2006-01-12 US US11/330,112 patent/US20060121519A1/en not_active Abandoned
- 2006-01-25 NO NO20060400A patent/NO20060400L/no not_active Application Discontinuation
Also Published As
| Publication number | Publication date |
|---|---|
| US20060121519A1 (en) | 2006-06-08 |
| EP1648995A2 (en) | 2006-04-26 |
| WO2005010141A2 (en) | 2005-02-03 |
| CA2531492A1 (en) | 2005-02-03 |
| ZA200600315B (en) | 2007-04-25 |
| EP1648995A4 (en) | 2010-03-10 |
| WO2005010141A3 (en) | 2009-03-26 |
| NO20060400L (no) | 2006-03-27 |
| KR20060037337A (ko) | 2006-05-03 |
| SG145760A1 (en) | 2008-09-29 |
| IL173107A0 (en) | 2006-06-11 |
| RU2006105648A (ru) | 2006-07-27 |
| CN101415721A (zh) | 2009-04-22 |
| JP2007515384A (ja) | 2007-06-14 |
| IL157086A0 (en) | 2004-02-08 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Turkova | Oriented immobilization of biologically active proteins as a tool for revealing protein interactions and function | |
| US7981632B2 (en) | Sequentially arranged streptavidin-binding modules as affinity tags | |
| Comer et al. | Characterization of a mouse monoclonal antibody specific for O-linked N-acetylglucosamine | |
| Kline | Handbook of affinity chromatography | |
| US7956165B2 (en) | Compositions and methods for purifying and crystallizing molecules of interest | |
| EP0871658B1 (en) | Modified avidin and streptavidin molecules and use thereof | |
| JPH05508701A (ja) | 被分析物に結合するリガンドの同定方法 | |
| MXPA06000944A (es) | Composiciones para purificar y cristalizar moleculas de interes. | |
| KR20210131323A (ko) | 우스테키누맙 생성 방법 | |
| WO2006085321A2 (en) | Compositions and methods for purifying and crystallizing molecules of interest | |
| Coleman et al. | Thermostabilization, expression, purification, and crystallization of the human serotonin transporter bound to S-citalopram | |
| Mohr et al. | Immunosorption techniques: fundamentals and applications | |
| AU2006200118A1 (en) | Compositions and Methods for Purifying and Crystallizing Molecules of Interest | |
| EP0206779A1 (en) | Detecting antinuclear antibody | |
| Eleniste et al. | Expression and characterization of an enantioselective antigen-binding fragment directed against α-amino acids | |
| WO2011068538A2 (en) | General method for generating ultra-high affinity binding proteins | |
| AU2007203370A1 (en) | Compositions and Methods for Purifying and Crystallizing Molecules of Interest | |
| Kassa | Production, characterization, and applications of stereoselective antibodies to α-hydroxy acids | |
| Carter | Production of Anti‐Peptide Antisera | |
| Czerwinski et al. | Construction of an agglutination tool: recombinant Fab fragments biotinylated in vitro | |
| CA1329545C (en) | Immunological complex, its preparation and its use | |
| KR101633791B1 (ko) | 수크라아제-이소말타아제에 대한 항체의 제조 방법 | |
| JPH03112493A (ja) | モノクローナル抗体およびそれを産生するハイブリドーマの製造方法 | |
| JPH02216459A (ja) | ハプテンである抗原に対し高親和性を持つ抗体 | |
| Wood | The discovery and development of the antigen-antibody reaction part 2: Commercial immunoassay development and applications |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FA | Abandonment or withdrawal |