CA2923704A1 - A method for analysing a sample of immunoglobulin molecules - Google Patents
A method for analysing a sample of immunoglobulin molecules Download PDFInfo
- Publication number
- CA2923704A1 CA2923704A1 CA2923704A CA2923704A CA2923704A1 CA 2923704 A1 CA2923704 A1 CA 2923704A1 CA 2923704 A CA2923704 A CA 2923704A CA 2923704 A CA2923704 A CA 2923704A CA 2923704 A1 CA2923704 A1 CA 2923704A1
- Authority
- CA
- Canada
- Prior art keywords
- polypeptide
- sample
- sequence
- analysing
- seq
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims abstract description 47
- 108060003951 Immunoglobulin Proteins 0.000 title claims abstract description 33
- 102000018358 immunoglobulin Human genes 0.000 title claims abstract description 33
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 142
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 110
- 229920001184 polypeptide Polymers 0.000 claims description 107
- 235000001014 amino acid Nutrition 0.000 claims description 30
- 239000000203 mixture Substances 0.000 claims description 27
- 150000001413 amino acids Chemical class 0.000 claims description 26
- 239000003814 drug Substances 0.000 claims description 24
- 241000282414 Homo sapiens Species 0.000 claims description 22
- 229940124597 therapeutic agent Drugs 0.000 claims description 22
- 239000012634 fragment Substances 0.000 claims description 21
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 19
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 claims description 15
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 claims description 15
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 13
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 13
- 238000004458 analytical method Methods 0.000 claims description 10
- 230000004481 post-translational protein modification Effects 0.000 claims description 10
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 claims description 7
- 108010005843 Cysteine Proteases Proteins 0.000 claims description 7
- 102000005927 Cysteine Proteases Human genes 0.000 claims description 7
- 230000004048 modification Effects 0.000 claims description 7
- 238000012986 modification Methods 0.000 claims description 7
- 238000004128 high performance liquid chromatography Methods 0.000 claims description 6
- AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 claims description 4
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 4
- -1 maytonsinoid Chemical compound 0.000 claims description 3
- 101710112752 Cytotoxin Proteins 0.000 claims description 2
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 claims description 2
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- 229960004679 doxorubicin Drugs 0.000 claims description 2
- 229960000485 methotrexate Drugs 0.000 claims description 2
- UOWVMDUEMSNCAV-WYENRQIDSA-N rachelmycin Chemical compound C1([C@]23C[C@@H]2CN1C(=O)C=1NC=2C(OC)=C(O)C4=C(C=2C=1)CCN4C(=O)C1=CC=2C=4CCN(C=4C(O)=C(C=2N1)OC)C(N)=O)=CC(=O)C1=C3C(C)=CN1 UOWVMDUEMSNCAV-WYENRQIDSA-N 0.000 claims description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 claims description 2
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 1
- HXCHCVDVKSCDHU-LULTVBGHSA-N calicheamicin Chemical compound C1[C@H](OC)[C@@H](NCC)CO[C@H]1O[C@H]1[C@H](O[C@@H]2C\3=C(NC(=O)OC)C(=O)C[C@](C/3=C/CSSSC)(O)C#C\C=C/C#C2)O[C@H](C)[C@@H](NO[C@@H]2O[C@H](C)[C@@H](SC(=O)C=3C(=C(OC)C(O[C@H]4[C@@H]([C@H](OC)[C@@H](O)[C@H](C)O4)O)=C(I)C=3C)OC)[C@@H](O)C2)[C@@H]1O HXCHCVDVKSCDHU-LULTVBGHSA-N 0.000 claims 1
- 238000000589 high-performance liquid chromatography-mass spectrometry Methods 0.000 claims 1
- 229940072221 immunoglobulins Drugs 0.000 abstract description 6
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- 229940049595 antibody-drug conjugate Drugs 0.000 description 9
- 230000000694 effects Effects 0.000 description 9
- 239000000611 antibody drug conjugate Substances 0.000 description 8
- 238000004949 mass spectrometry Methods 0.000 description 8
- 239000003638 chemical reducing agent Substances 0.000 description 6
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 6
- 125000001931 aliphatic group Chemical group 0.000 description 5
- 229960000455 brentuximab vedotin Drugs 0.000 description 5
- 239000011347 resin Substances 0.000 description 5
- 229920005989 resin Polymers 0.000 description 5
- 238000006467 substitution reaction Methods 0.000 description 5
- 241000194017 Streptococcus Species 0.000 description 4
- 125000003118 aryl group Chemical group 0.000 description 4
- 229940120638 avastin Drugs 0.000 description 4
- 239000011230 binding agent Substances 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 238000012512 characterization method Methods 0.000 description 4
- 239000004365 Protease Substances 0.000 description 3
- PZBFGYYEXUXCOF-UHFFFAOYSA-N TCEP Chemical compound OC(=O)CCP(CCC(O)=O)CCC(O)=O PZBFGYYEXUXCOF-UHFFFAOYSA-N 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
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- 238000000926 separation method Methods 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 241001468181 Streptococcus sp. 'group C' Species 0.000 description 2
- 238000005251 capillar electrophoresis Methods 0.000 description 2
- 238000003981 capillary liquid chromatography Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 238000001499 laser induced fluorescence spectroscopy Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 235000019419 proteases Nutrition 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 238000001542 size-exclusion chromatography Methods 0.000 description 2
- 229940126622 therapeutic monoclonal antibody Drugs 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- ATRRKUHOCOJYRX-UHFFFAOYSA-N Ammonium bicarbonate Chemical compound [NH4+].OC([O-])=O ATRRKUHOCOJYRX-UHFFFAOYSA-N 0.000 description 1
- 229910000013 Ammonium bicarbonate Inorganic materials 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 150000008574 D-amino acids Chemical class 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 239000007987 MES buffer Substances 0.000 description 1
- 108010080638 N-benzyloxycarbonyl-leucyl-valyl-glycine diazomethane Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 101710121155 Poly(A) polymerase I Proteins 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 241000589776 Pseudomonas putida Species 0.000 description 1
- ODHCTXKNWHHXJC-GSVOUGTGSA-N Pyroglutamic acid Natural products OC(=O)[C@H]1CCC(=O)N1 ODHCTXKNWHHXJC-GSVOUGTGSA-N 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 241000120569 Streptococcus equi subsp. zooepidemicus Species 0.000 description 1
- 241001505901 Streptococcus sp. 'group A' Species 0.000 description 1
- 241000194005 Streptococcus sp. 'group G' Species 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- ODHCTXKNWHHXJC-UHFFFAOYSA-N acide pyroglutamique Natural products OC(=O)C1CCC(=O)N1 ODHCTXKNWHHXJC-UHFFFAOYSA-N 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 235000012538 ammonium bicarbonate Nutrition 0.000 description 1
- 239000001099 ammonium carbonate Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 238000010504 bond cleavage reaction Methods 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000006240 deamidation Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 108010022946 erythrogenic toxin Proteins 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 150000004676 glycans Chemical group 0.000 description 1
- 230000036252 glycation Effects 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 238000006317 isomerization reaction Methods 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 239000008024 pharmaceutical diluent Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
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- 239000011780 sodium chloride Substances 0.000 description 1
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- 125000001424 substituent group Chemical group 0.000 description 1
- 238000012360 testing method Methods 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
- 238000001195 ultra high performance liquid chromatography Methods 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
- G01N33/6857—Antibody fragments
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6854—Immunoglobulins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6472—Cysteine endopeptidases (3.4.22)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6848—Methods of protein analysis involving mass spectrometry
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
- C07K2317/53—Hinge
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/22—Cysteine endopeptidases (3.4.22)
- C12Y304/2201—Streptopain (3.4.22.10)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
- G01N2333/964—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue
- G01N2333/96402—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from non-mammals
- G01N2333/96405—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from non-mammals in general
- G01N2333/96408—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from non-mammals in general with EC number
- G01N2333/96413—Cysteine endopeptidases (3.4.22)
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2560/00—Chemical aspects of mass spectrometric analysis of biological material
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Genetics & Genomics (AREA)
- Physics & Mathematics (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Wood Science & Technology (AREA)
- Pathology (AREA)
- Analytical Chemistry (AREA)
- Food Science & Technology (AREA)
- Cell Biology (AREA)
- General Physics & Mathematics (AREA)
- General Engineering & Computer Science (AREA)
- Biophysics (AREA)
- Bioinformatics & Computational Biology (AREA)
- Spectroscopy & Molecular Physics (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB1316744.0 | 2013-09-20 | ||
| GBGB1316744.0A GB201316744D0 (en) | 2013-09-20 | 2013-09-20 | Method |
| PCT/EP2014/069920 WO2015040125A1 (en) | 2013-09-20 | 2014-09-18 | A method for analysing a sample of immunoglobulin molecules |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2923704A1 true CA2923704A1 (en) | 2015-03-26 |
Family
ID=49553168
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2923704A Abandoned CA2923704A1 (en) | 2013-09-20 | 2014-09-18 | A method for analysing a sample of immunoglobulin molecules |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US20160231329A1 (enExample) |
| EP (1) | EP3047280A1 (enExample) |
| JP (1) | JP2016531546A (enExample) |
| KR (1) | KR20160079784A (enExample) |
| AU (1) | AU2014323081A1 (enExample) |
| CA (1) | CA2923704A1 (enExample) |
| GB (1) | GB201316744D0 (enExample) |
| SG (1) | SG11201602138VA (enExample) |
| WO (1) | WO2015040125A1 (enExample) |
Families Citing this family (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU1686302A (en) * | 2000-12-21 | 2002-07-01 | Shire Biochem Inc | Streptococcus pyogenes antigens and corresponding dna fragments |
| US10267806B2 (en) | 2014-04-04 | 2019-04-23 | Mayo Foundation For Medical Education And Research | Isotyping immunoglobulins using accurate molecular mass |
| GB201502306D0 (en) | 2015-02-12 | 2015-04-01 | Hansa Medical Ab | Protein |
| GB201502305D0 (en) | 2015-02-12 | 2015-04-01 | Hansa Medical Ab | Protein |
| US11209439B2 (en) | 2015-09-24 | 2021-12-28 | Mayo Foundation For Medical Education And Research | Identification of immunoglobulin free light chains by mass spectrometry |
| CN108291913B (zh) | 2015-12-09 | 2021-08-17 | 豪夫迈·罗氏有限公司 | 确定体内相互作用模式的方法 |
| CN108369232B (zh) | 2015-12-09 | 2022-05-31 | 豪夫迈·罗氏有限公司 | 人IgG1结合多聚抗原的直接亲和力测量 |
| WO2017134274A1 (en) * | 2016-02-04 | 2017-08-10 | Ulrich Von Pawel-Rammingen | New streptococcal proteases |
| WO2017205741A1 (en) | 2016-05-27 | 2017-11-30 | Genentech, Inc. | Bioanalytical method for the characterization of site-specific antibody-drug conjugates |
| US10955420B2 (en) | 2016-09-07 | 2021-03-23 | Mayo Foundation For Medical Education And Research | Identification and monitoring of cleaved immunoglobulins by molecular mass |
| WO2018093868A1 (en) * | 2016-11-16 | 2018-05-24 | University Of Florida Research Foundation, Inc. | Immunoglobulin proteases, compositions, and uses thereof |
| ES2986557T3 (es) | 2017-05-26 | 2024-11-11 | Genovis Ab | Enzimas para el análisis de glucanos |
| US11946937B2 (en) | 2017-09-13 | 2024-04-02 | Mayo Foundation For Medical Education And Research | Identification and monitoring of apoptosis inhibitor of macrophage |
| US12153052B2 (en) | 2017-09-13 | 2024-11-26 | Mayo Foundation For Medical Education And Research | Identification and monitoring of immunoglobulin J chains |
| EP4079848A1 (en) * | 2021-04-22 | 2022-10-26 | Genovis Ab | Immunoglobulin cleaving enzyme |
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| US5965709A (en) * | 1991-08-14 | 1999-10-12 | Genentech, Inc. | IgE antagonists |
| GB0130228D0 (en) * | 2001-12-18 | 2002-02-06 | Hansa Medica Ab | Protein |
| WO2013033008A2 (en) * | 2011-08-26 | 2013-03-07 | Merrimack Pharmaceuticals, Inc. | Tandem fc bispecific antibodies |
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2013
- 2013-09-20 GB GBGB1316744.0A patent/GB201316744D0/en not_active Ceased
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2014
- 2014-09-18 CA CA2923704A patent/CA2923704A1/en not_active Abandoned
- 2014-09-18 SG SG11201602138VA patent/SG11201602138VA/en unknown
- 2014-09-18 US US15/023,042 patent/US20160231329A1/en not_active Abandoned
- 2014-09-18 EP EP14772310.0A patent/EP3047280A1/en not_active Withdrawn
- 2014-09-18 AU AU2014323081A patent/AU2014323081A1/en not_active Abandoned
- 2014-09-18 WO PCT/EP2014/069920 patent/WO2015040125A1/en not_active Ceased
- 2014-09-18 KR KR1020167010252A patent/KR20160079784A/ko not_active Withdrawn
- 2014-09-18 JP JP2016515415A patent/JP2016531546A/ja not_active Withdrawn
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| SG11201602138VA (en) | 2016-04-28 |
| GB201316744D0 (en) | 2013-11-06 |
| JP2016531546A (ja) | 2016-10-13 |
| US20160231329A1 (en) | 2016-08-11 |
| KR20160079784A (ko) | 2016-07-06 |
| AU2014323081A1 (en) | 2016-03-31 |
| WO2015040125A1 (en) | 2015-03-26 |
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| Date | Code | Title | Description |
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