CA2471346A1 - Method for protein expression analysis - Google Patents
Method for protein expression analysis Download PDFInfo
- Publication number
- CA2471346A1 CA2471346A1 CA002471346A CA2471346A CA2471346A1 CA 2471346 A1 CA2471346 A1 CA 2471346A1 CA 002471346 A CA002471346 A CA 002471346A CA 2471346 A CA2471346 A CA 2471346A CA 2471346 A1 CA2471346 A1 CA 2471346A1
- Authority
- CA
- Canada
- Prior art keywords
- protein
- cells
- peptides
- labelled
- reagent
- 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
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 117
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 115
- 238000000034 method Methods 0.000 title claims abstract description 99
- 238000010195 expression analysis Methods 0.000 title description 5
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 116
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 81
- 239000003153 chemical reaction reagent Substances 0.000 claims abstract description 66
- 238000004949 mass spectrometry Methods 0.000 claims abstract description 37
- 239000000203 mixture Substances 0.000 claims abstract description 35
- 238000004458 analytical method Methods 0.000 claims abstract description 29
- 238000002372 labelling Methods 0.000 claims abstract description 27
- 239000012634 fragment Substances 0.000 claims abstract description 24
- 230000007935 neutral effect Effects 0.000 claims abstract description 15
- 238000000148 multi-dimensional chromatography Methods 0.000 claims abstract 2
- 235000018102 proteins Nutrition 0.000 claims description 101
- 238000001228 spectrum Methods 0.000 claims description 22
- 150000002500 ions Chemical class 0.000 claims description 17
- 229920001184 polypeptide Polymers 0.000 claims description 14
- 239000011230 binding agent Substances 0.000 claims description 11
- 108010052285 Membrane Proteins Proteins 0.000 claims description 10
- 230000029087 digestion Effects 0.000 claims description 10
- 230000000155 isotopic effect Effects 0.000 claims description 10
- 150000001413 amino acids Chemical group 0.000 claims description 9
- 239000012528 membrane Substances 0.000 claims description 7
- 150000001412 amines Chemical class 0.000 claims description 6
- 235000018417 cysteine Nutrition 0.000 claims description 6
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 6
- 229940070376 protein Drugs 0.000 claims description 6
- XVGZBALMNMZTIO-UHFFFAOYSA-N 2-[[1-(2,5-dioxopyrrolidin-1-yl)-2H-pyridin-4-yl]methylsulfanyl]acetic acid Chemical group C1=CC(CSCC(=O)O)=CCN1N1C(=O)CCC1=O XVGZBALMNMZTIO-UHFFFAOYSA-N 0.000 claims description 5
- 102000018697 Membrane Proteins Human genes 0.000 claims description 5
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 claims description 5
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 claims description 3
- 238000001323 two-dimensional chromatography Methods 0.000 claims description 3
- 108010051815 Glutamyl endopeptidase Proteins 0.000 claims description 2
- 108010030544 Peptidyl-Lys metalloendopeptidase Proteins 0.000 claims description 2
- 238000005040 ion trap Methods 0.000 claims description 2
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 claims 2
- 238000004366 reverse phase liquid chromatography Methods 0.000 claims 2
- 235000019333 sodium laurylsulphate Nutrition 0.000 claims 2
- 238000005571 anion exchange chromatography Methods 0.000 claims 1
- 238000000605 extraction Methods 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 49
- 238000012790 confirmation Methods 0.000 description 20
- 238000000926 separation method Methods 0.000 description 11
- 238000001514 detection method Methods 0.000 description 9
- 238000004885 tandem mass spectrometry Methods 0.000 description 9
- 239000000126 substance Substances 0.000 description 8
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 241000282414 Homo sapiens Species 0.000 description 6
- 235000001014 amino acid Nutrition 0.000 description 6
- 238000004587 chromatography analysis Methods 0.000 description 6
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- 230000007017 scission Effects 0.000 description 6
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 5
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 5
- 239000004473 Threonine Substances 0.000 description 5
- 239000002253 acid Substances 0.000 description 5
- 239000007789 gas Substances 0.000 description 5
- 229910019142 PO4 Inorganic materials 0.000 description 4
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 4
- 125000003277 amino group Chemical group 0.000 description 4
- 125000004429 atom Chemical group 0.000 description 4
- 230000006870 function Effects 0.000 description 4
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- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 4
- 239000010452 phosphate Substances 0.000 description 4
- 239000003223 protective agent Substances 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- FYSNRJHAOHDILO-UHFFFAOYSA-N thionyl chloride Chemical compound ClS(Cl)=O FYSNRJHAOHDILO-UHFFFAOYSA-N 0.000 description 4
- 238000000539 two dimensional gel electrophoresis Methods 0.000 description 4
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- 238000001261 affinity purification Methods 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 235000018977 lysine Nutrition 0.000 description 3
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- DXBJXKJWSYXGLZ-UHFFFAOYSA-N 1-pyridin-2-ylethanethiol Chemical compound CC(S)C1=CC=CC=N1 DXBJXKJWSYXGLZ-UHFFFAOYSA-N 0.000 description 2
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
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- 108010015899 Glycopeptides Proteins 0.000 description 2
- 102000002068 Glycopeptides Human genes 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 2
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 2
- PVNIIMVLHYAWGP-UHFFFAOYSA-N Niacin Chemical compound OC(=O)C1=CC=CN=C1 PVNIIMVLHYAWGP-UHFFFAOYSA-N 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 108010001441 Phosphopeptides Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 108010026552 Proteome Proteins 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 208000032005 Spinocerebellar ataxia with axonal neuropathy type 2 Diseases 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 150000001263 acyl chlorides Chemical class 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 208000033361 autosomal recessive with axonal neuropathy 2 spinocerebellar ataxia Diseases 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 238000005515 capillary zone electrophoresis Methods 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 238000001212 derivatisation Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
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- 230000006862 enzymatic digestion Effects 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 238000002013 hydrophilic interaction chromatography Methods 0.000 description 2
- 230000002209 hydrophobic effect Effects 0.000 description 2
- 125000003588 lysine group Chemical class [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
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- 230000004481 post-translational protein modification Effects 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
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- 238000004445 quantitative analysis Methods 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 238000007086 side reaction Methods 0.000 description 2
- 230000035322 succinylation Effects 0.000 description 2
- 238000010613 succinylation reaction Methods 0.000 description 2
- 230000020382 suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Effects 0.000 description 2
- YEDDVXZFXSHDIB-UHFFFAOYSA-N 1,1,2,2,3,3-hexafluoropropan-1-ol Chemical compound OC(F)(F)C(F)(F)C(F)F YEDDVXZFXSHDIB-UHFFFAOYSA-N 0.000 description 1
- PPHIIIRFJKDTLG-UHFFFAOYSA-N 1-pyridin-2-ylethanol Chemical compound CC(O)C1=CC=CC=N1 PPHIIIRFJKDTLG-UHFFFAOYSA-N 0.000 description 1
- FALRKNHUBBKYCC-UHFFFAOYSA-N 2-(chloromethyl)pyridine-3-carbonitrile Chemical compound ClCC1=NC=CC=C1C#N FALRKNHUBBKYCC-UHFFFAOYSA-N 0.000 description 1
- 238000006218 Arndt-Eistert homologation reaction Methods 0.000 description 1
- 101100421200 Caenorhabditis elegans sep-1 gene Proteins 0.000 description 1
- -1 Cys or Met Chemical class 0.000 description 1
- YZCKVEUIGOORGS-OUBTZVSYSA-N Deuterium Chemical compound [2H] YZCKVEUIGOORGS-OUBTZVSYSA-N 0.000 description 1
- YXHKONLOYHBTNS-UHFFFAOYSA-N Diazomethane Chemical compound C=[N+]=[N-] YXHKONLOYHBTNS-UHFFFAOYSA-N 0.000 description 1
- QOSSAOTZNIDXMA-UHFFFAOYSA-N Dicylcohexylcarbodiimide Chemical compound C1CCCCC1N=C=NC1CCCCC1 QOSSAOTZNIDXMA-UHFFFAOYSA-N 0.000 description 1
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 1
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 125000002842 L-seryl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])O[H] 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 101710190786 PI protein Proteins 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- 102000016611 Proteoglycans Human genes 0.000 description 1
- 108010067787 Proteoglycans Proteins 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 101000829189 Staphylococcus aureus Glutamyl endopeptidase Proteins 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000003314 affinity selection Methods 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 150000004982 aromatic amines Chemical class 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N aspartic acid group Chemical group N[C@@H](CC(=O)O)C(=O)O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
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- 238000003981 capillary liquid chromatography Methods 0.000 description 1
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- 238000005119 centrifugation Methods 0.000 description 1
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000004182 chemical digestion Methods 0.000 description 1
- 125000003636 chemical group Chemical group 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000004891 communication Methods 0.000 description 1
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- 150000001875 compounds Chemical class 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000003436 cytoskeletal effect Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000010511 deprotection reaction Methods 0.000 description 1
- 229910052805 deuterium Inorganic materials 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 229940124568 digestive agent Drugs 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
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- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
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- 239000012039 electrophile Substances 0.000 description 1
- 238000000132 electrospray ionisation Methods 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethanethiol Chemical compound CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 229940093499 ethyl acetate Drugs 0.000 description 1
- 235000019439 ethyl acetate Nutrition 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 239000000727 fraction Substances 0.000 description 1
- ZZUFCTLCJUWOSV-UHFFFAOYSA-N furosemide Chemical compound C1=C(Cl)C(S(=O)(=O)N)=CC(C(O)=O)=C1NCC1=CC=CO1 ZZUFCTLCJUWOSV-UHFFFAOYSA-N 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 238000000589 high-performance liquid chromatography-mass spectrometry Methods 0.000 description 1
- BHEPBYXIRTUNPN-UHFFFAOYSA-N hydridophosphorus(.) (triplet) Chemical compound [PH] BHEPBYXIRTUNPN-UHFFFAOYSA-N 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 238000013383 initial experiment Methods 0.000 description 1
- JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 1
- 238000001294 liquid chromatography-tandem mass spectrometry Methods 0.000 description 1
- 239000012280 lithium aluminium hydride Substances 0.000 description 1
- 238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 238000001186 nanoelectrospray ionisation mass spectrometry Methods 0.000 description 1
- 235000001968 nicotinic acid Nutrition 0.000 description 1
- 229960003512 nicotinic acid Drugs 0.000 description 1
- 239000011664 nicotinic acid Substances 0.000 description 1
- 229910052757 nitrogen Inorganic materials 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
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- HEGSGKPQLMEBJL-RKQHYHRCSA-N octyl beta-D-glucopyranoside Chemical compound CCCCCCCCO[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O HEGSGKPQLMEBJL-RKQHYHRCSA-N 0.000 description 1
- 230000010355 oscillation Effects 0.000 description 1
- 238000002542 parent ion scan Methods 0.000 description 1
- YPJUNDFVDDCYIH-UHFFFAOYSA-N perfluorobutyric acid Chemical compound OC(=O)C(F)(F)C(F)(F)C(F)(F)F YPJUNDFVDDCYIH-UHFFFAOYSA-N 0.000 description 1
- 102000005681 phospholamban Human genes 0.000 description 1
- 108010059929 phospholamban Proteins 0.000 description 1
- BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 1
- 238000012805 post-processing Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000001953 recrystallisation Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000000284 resting effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- VGGUKFAVHPGNBF-UHFFFAOYSA-N s-ethyl 2,2,2-trifluoroethanethioate Chemical compound CCSC(=O)C(F)(F)F VGGUKFAVHPGNBF-UHFFFAOYSA-N 0.000 description 1
- 210000001908 sarcoplasmic reticulum Anatomy 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- CLDWGXZGFUNWKB-UHFFFAOYSA-M silver;benzoate Chemical compound [Ag+].[O-]C(=O)C1=CC=CC=C1 CLDWGXZGFUNWKB-UHFFFAOYSA-M 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- HYHCSLBZRBJJCH-UHFFFAOYSA-M sodium hydrosulfide Chemical compound [Na+].[SH-] HYHCSLBZRBJJCH-UHFFFAOYSA-M 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000010183 spectrum analysis Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000002305 strong-anion-exchange chromatography Methods 0.000 description 1
- 229940014800 succinic anhydride Drugs 0.000 description 1
- 230000001629 suppression Effects 0.000 description 1
- 210000001179 synovial fluid Anatomy 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 150000003573 thiols Chemical class 0.000 description 1
- HFRXJVQOXRXOPP-UHFFFAOYSA-N thionyl bromide Chemical compound BrS(Br)=O HFRXJVQOXRXOPP-UHFFFAOYSA-N 0.000 description 1
- 229910052718 tin Inorganic materials 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 238000001419 two-dimensional polyacrylamide gel electrophoresis Methods 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 238000012800 visualization 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
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Hematology (AREA)
- Chemical & Material Sciences (AREA)
- Urology & Nephrology (AREA)
- Physics & Mathematics (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Bioinformatics & Computational Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Food Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Cell Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Other Investigation Or Analysis Of Materials By Electrical Means (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB0130845.1A GB0130845D0 (en) | 2001-12-22 | 2001-12-22 | Analysis |
| GB0130845.1 | 2001-12-22 | ||
| PCT/EP2002/014328 WO2003056343A2 (en) | 2001-12-22 | 2002-12-16 | Method for protein expression analysis |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2471346A1 true CA2471346A1 (en) | 2003-07-10 |
Family
ID=9928324
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002471346A Abandoned CA2471346A1 (en) | 2001-12-22 | 2002-12-16 | Method for protein expression analysis |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US20050164336A1 (https=) |
| EP (1) | EP1472542A2 (https=) |
| JP (1) | JP2005513507A (https=) |
| AU (1) | AU2002364749A1 (https=) |
| CA (1) | CA2471346A1 (https=) |
| GB (1) | GB0130845D0 (https=) |
| WO (1) | WO2003056343A2 (https=) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4613299B2 (ja) | 2003-01-30 | 2011-01-12 | ディーエイチ テクノロジーズ デベロップメント プライベート リミテッド | 分析物分析に関する方法、混合物、キット、および組成物 |
| GB0314209D0 (en) * | 2003-06-19 | 2003-07-23 | Amersham Biosciences Ab | Novel MS reagents |
| WO2005012247A1 (en) * | 2003-07-30 | 2005-02-10 | Hôpital Sainte-Justine | Compounds and methods for the rapid quantitative analysis of proteins and polypeptides |
| WO2005015239A2 (en) * | 2003-08-07 | 2005-02-17 | Cornell Research Foundation, Inc. | Method for n-terminal labeling of proteins |
| DE10340521B4 (de) * | 2003-09-03 | 2012-01-05 | Bruker Daltonik Gmbh | Verfahren selektiver Kapillarelektrophorese |
| CA2542941C (en) * | 2003-11-26 | 2013-02-12 | Applera Corporation | Analysis of mass spectral data in the quiet zones and label selection therefor |
| EP1916527A1 (en) * | 2003-11-26 | 2008-04-30 | Applera Corporation | Analysis of mass spectral data in the quiet zones |
| US20050148087A1 (en) | 2004-01-05 | 2005-07-07 | Applera Corporation | Isobarically labeled analytes and fragment ions derived therefrom |
| KR100611313B1 (ko) * | 2004-06-30 | 2006-08-10 | 고려대학교 산학협력단 | 폴리펩티드의 ｎ-말단 치환용 화합물, 이를 이용한폴리펩티드 내의 아미노산 서열분석 및 정량방법 |
| US8105838B2 (en) * | 2005-06-03 | 2012-01-31 | Waters Technologies Corporation | Generation and use of a catalog of polypeptide-related information for chemical analyses |
| JP4724816B2 (ja) * | 2005-09-06 | 2011-07-13 | シャープ株式会社 | タンパク質の測定方法 |
| JP5003274B2 (ja) * | 2007-05-16 | 2012-08-15 | 株式会社日立製作所 | 質量分析システムおよび質量分析方法 |
| WO2010033508A1 (en) | 2008-09-16 | 2010-03-25 | Historx, Inc. | Reproducible quantification of biomarker expression |
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|---|---|---|---|---|
| GB9223168D0 (en) * | 1992-11-05 | 1992-12-16 | Johnson Matthey Plc | Improvements in molecule labelling |
| AUPQ664300A0 (en) * | 2000-04-03 | 2000-05-04 | Proteome Systems Ltd | Macromolecule detection |
| GB0123858D0 (en) * | 2001-10-05 | 2001-11-28 | James Peter | Method for analysing protein/peptide expression |
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- 2002-12-16 WO PCT/EP2002/014328 patent/WO2003056343A2/en not_active Ceased
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- 2002-12-16 EP EP02805756A patent/EP1472542A2/en not_active Withdrawn
- 2002-12-16 AU AU2002364749A patent/AU2002364749A1/en not_active Abandoned
- 2002-12-16 US US10/499,885 patent/US20050164336A1/en not_active Abandoned
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| AU2002364749A8 (en) | 2003-07-15 |
| AU2002364749A1 (en) | 2003-07-15 |
| WO2003056343B1 (en) | 2004-12-16 |
| WO2003056343A3 (en) | 2004-08-26 |
| EP1472542A2 (en) | 2004-11-03 |
| GB0130845D0 (en) | 2002-02-06 |
| JP2005513507A (ja) | 2005-05-12 |
| WO2003056343A2 (en) | 2003-07-10 |
| US20050164336A1 (en) | 2005-07-28 |
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