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
- 238000003776 cleavage reaction Methods 0.000 description 6
- 210000004379 membrane Anatomy 0.000 description 6
- 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
- 238000001948 isotopic labelling Methods 0.000 description 4
- 239000003550 marker Substances 0.000 description 4
- 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
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 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
- 238000011161 development Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 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
- 238000012986 modification Methods 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 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
- 239000010839 body fluid Substances 0.000 description 1
- 238000003981 capillary liquid chromatography Methods 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 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
- 239000002131 composite material Substances 0.000 description 1
- 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
- 239000012895 dilution Substances 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000004821 distillation Methods 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 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 |
|---|---|---|---|
| GB0130845.1 | 2001-12-22 | ||
| GBGB0130845.1A GB0130845D0 (en) | 2001-12-22 | 2001-12-22 | Analysis |
| 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 (enExample) |
| EP (1) | EP1472542A2 (enExample) |
| JP (1) | JP2005513507A (enExample) |
| AU (1) | AU2002364749A1 (enExample) |
| CA (1) | CA2471346A1 (enExample) |
| GB (1) | GB0130845D0 (enExample) |
| WO (1) | WO2003056343A2 (enExample) |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20040219685A1 (en) | 2003-01-30 | 2004-11-04 | Applera Corporation | Methods and mixtures pertaining to analyte determination using electrophilic labeling reagents |
| 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 |
| DE602004009824T2 (de) * | 2003-11-26 | 2008-03-06 | Applera Corp., Framingham | Analyse von massenspektraldaten in den ruhigen gebieten |
| 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 |
| JP5011283B2 (ja) * | 2005-06-03 | 2012-08-29 | ウオーターズ・テクノロジーズ・コーポレイシヨン | 化学分析のためのポリペプチド関連情報のカタログの発生および使用 |
| 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 |
| US9240043B2 (en) | 2008-09-16 | 2016-01-19 | Novartis Ag | Reproducible quantification of biomarker expression |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
-
2001
- 2001-12-22 GB GBGB0130845.1A patent/GB0130845D0/en not_active Ceased
-
2002
- 2002-12-16 JP JP2003556815A patent/JP2005513507A/ja active Pending
- 2002-12-16 WO PCT/EP2002/014328 patent/WO2003056343A2/en not_active Ceased
- 2002-12-16 US US10/499,885 patent/US20050164336A1/en not_active Abandoned
- 2002-12-16 AU AU2002364749A patent/AU2002364749A1/en not_active Abandoned
- 2002-12-16 EP EP02805756A patent/EP1472542A2/en not_active Withdrawn
- 2002-12-16 CA CA002471346A patent/CA2471346A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| JP2005513507A (ja) | 2005-05-12 |
| AU2002364749A1 (en) | 2003-07-15 |
| WO2003056343B1 (en) | 2004-12-16 |
| WO2003056343A3 (en) | 2004-08-26 |
| EP1472542A2 (en) | 2004-11-03 |
| AU2002364749A8 (en) | 2003-07-15 |
| US20050164336A1 (en) | 2005-07-28 |
| GB0130845D0 (en) | 2002-02-06 |
| WO2003056343A2 (en) | 2003-07-10 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4300029B2 (ja) | ゲルフリー定性及び定量的プロテオーム分析のための方法及び装置、ならびにその使用 | |
| Righetti et al. | Quantitative proteomics: a review of different methodologies | |
| CN101600959B (zh) | 肽和蛋白的定量方法 | |
| US6629040B1 (en) | Isotope distribution encoded tags for protein identification | |
| US20100068819A1 (en) | Compounds and methods for double labelling of polypeptides to allow multiplexing in mass spectrometric analysis | |
| JP2003532900A (ja) | タンパク質を同定及び定量化するための親和性により選択されるサインペプチド | |
| CA2471346A1 (en) | Method for protein expression analysis | |
| AU2004292202A1 (en) | Fluorous labeling for selective processing of biologically-derived samples | |
| Nakazawa et al. | Terminal proteomics: N‐and C‐terminal analyses for high‐fidelity identification of proteins using MS | |
| JP2004516486A (ja) | マーカー／標的タンパク質を迅速に同定するための逆標識方法 | |
| Li et al. | Simultaneous enrichment and sequential separation of O-linked glycopeptides and phosphopeptides with immobilized titanium (IV) ion affinity chromatography materials | |
| CN111777696A (zh) | 一种特异性可逆富集新生蛋白质的方法 | |
| Li et al. | CILAT–a new reagent for quantitative proteomics | |
| US20050042676A1 (en) | Characterising polypeptides | |
| JP2005189232A (ja) | 複合体混合物中のタンパク質の同定と定量的分析のための選択的ペプチド単離法 | |
| WO2008032235A2 (en) | Methods for analysing protein samples based on the identification of c-terminal peptides | |
| WO2008056290A9 (en) | Use of arylboronic acids in protein labelling | |
| US7943029B2 (en) | Method, composition and kit for isoelectric focusing | |
| EP1459073B1 (en) | Method for determining molecule-molecule interaction in proteomics | |
| CN101535812A (zh) | 蛋白水解加工的质谱法分析 | |
| EP1916526A1 (en) | Method for diagnostic and therapeutic target discovery by combining isotopic and isobaric labels | |
| WO2003031982A1 (en) | Method for analysing protein/peptide expression | |
| Castagna et al. | Prefractionation of urinary proteins | |
| Stone et al. | Identification of proteins based on MS/MS spectra and location of posttranslational modifications | |
| Larsen et al. | Phosphoproteomics |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |