JP2005221328A - 糖鎖構造解析手法 - Google Patents
糖鎖構造解析手法 Download PDFInfo
- Publication number
- JP2005221328A JP2005221328A JP2004028324A JP2004028324A JP2005221328A JP 2005221328 A JP2005221328 A JP 2005221328A JP 2004028324 A JP2004028324 A JP 2004028324A JP 2004028324 A JP2004028324 A JP 2004028324A JP 2005221328 A JP2005221328 A JP 2005221328A
- Authority
- JP
- Japan
- Prior art keywords
- sugar chain
- sugar
- labeled
- galactose
- analysis method
- 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.)
- Granted
Links
- 235000000346 sugar Nutrition 0.000 title claims abstract description 206
- 238000003696 structure analysis method Methods 0.000 title claims abstract description 16
- 238000004458 analytical method Methods 0.000 claims description 14
- 238000000034 method Methods 0.000 claims description 10
- 238000012916 structural analysis Methods 0.000 claims description 3
- 238000004949 mass spectrometry Methods 0.000 abstract description 7
- 238000002372 labelling Methods 0.000 abstract description 5
- 150000002500 ions Chemical class 0.000 description 34
- 229930182830 galactose Natural products 0.000 description 27
- 239000012634 fragment Substances 0.000 description 25
- 239000002243 precursor Substances 0.000 description 20
- 238000006243 chemical reaction Methods 0.000 description 16
- 238000001228 spectrum Methods 0.000 description 13
- XCCTYIAWTASOJW-UHFFFAOYSA-N UDP-Glc Natural products OC1C(O)C(COP(O)(=O)OP(O)(O)=O)OC1N1C(=O)NC(=O)C=C1 XCCTYIAWTASOJW-UHFFFAOYSA-N 0.000 description 11
- 239000002994 raw material Substances 0.000 description 10
- 239000011734 sodium Substances 0.000 description 10
- 238000005481 NMR spectroscopy Methods 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- XCCTYIAWTASOJW-XVFCMESISA-N Uridine-5'-Diphosphate Chemical compound O[C@@H]1[C@H](O)[C@@H](COP(O)(=O)OP(O)(O)=O)O[C@H]1N1C(=O)NC(=O)C=C1 XCCTYIAWTASOJW-XVFCMESISA-N 0.000 description 8
- 238000006366 phosphorylation reaction Methods 0.000 description 7
- HSCJRCZFDFQWRP-JZMIEXBBSA-N UDP-alpha-D-glucose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-JZMIEXBBSA-N 0.000 description 5
- HSCJRCZFDFQWRP-UHFFFAOYSA-N Uridindiphosphoglukose Natural products OC1C(O)C(O)C(CO)OC1OP(O)(=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-UHFFFAOYSA-N 0.000 description 5
- HXXFSFRBOHSIMQ-FPRJBGLDSA-N alpha-D-galactose 1-phosphate Chemical compound OC[C@H]1O[C@H](OP(O)(O)=O)[C@H](O)[C@@H](O)[C@H]1O HXXFSFRBOHSIMQ-FPRJBGLDSA-N 0.000 description 5
- 238000003776 cleavage reaction Methods 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- ZKHQWZAMYRWXGA-KQYNXXCUSA-N Adenosine triphosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-N 0.000 description 4
- ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 description 4
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 4
- DTBNBXWJWCWCIK-UHFFFAOYSA-N Phosphoenolpyruvic acid Natural products OC(=O)C(=C)OP(O)(O)=O DTBNBXWJWCWCIK-UHFFFAOYSA-N 0.000 description 4
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 4
- DRTQHJPVMGBUCF-XVFCMESISA-N Uridine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-XVFCMESISA-N 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 239000008103 glucose Substances 0.000 description 4
- 229930182478 glucoside Natural products 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- 238000005918 transglycosylation reaction Methods 0.000 description 4
- 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 3
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 102000030902 Galactosyltransferase Human genes 0.000 description 3
- 108060003306 Galactosyltransferase Proteins 0.000 description 3
- 108010009595 Inorganic Pyrophosphatase Proteins 0.000 description 3
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical compound C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 description 3
- OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 3
- MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 description 3
- 102000013009 Pyruvate Kinase Human genes 0.000 description 3
- 108020005115 Pyruvate Kinase Proteins 0.000 description 3
- 102000004357 Transferases Human genes 0.000 description 3
- 108090000992 Transferases Proteins 0.000 description 3
- PGAVKCOVUIYSFO-XVFCMESISA-N UTP Chemical compound O[C@@H]1[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O[C@H]1N1C(=O)NC(=O)C=C1 PGAVKCOVUIYSFO-XVFCMESISA-N 0.000 description 3
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical group OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 3
- 150000001720 carbohydrates Chemical group 0.000 description 3
- 238000006209 dephosphorylation reaction Methods 0.000 description 3
- 235000011180 diphosphates Nutrition 0.000 description 3
- 238000001948 isotopic labelling Methods 0.000 description 3
- 229930029653 phosphoenolpyruvate Natural products 0.000 description 3
- 230000026731 phosphorylation Effects 0.000 description 3
- 239000002904 solvent Substances 0.000 description 3
- PGAVKCOVUIYSFO-UHFFFAOYSA-N uridine-triphosphate Natural products OC1C(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)OC1N1C(=O)NC(=O)C=C1 PGAVKCOVUIYSFO-UHFFFAOYSA-N 0.000 description 3
- XTWYTFMLZFPYCI-KQYNXXCUSA-N 5'-adenylphosphoric acid Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O XTWYTFMLZFPYCI-KQYNXXCUSA-N 0.000 description 2
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 2
- 102000048120 Galactokinases Human genes 0.000 description 2
- 108700023157 Galactokinases Proteins 0.000 description 2
- 102000051366 Glycosyltransferases Human genes 0.000 description 2
- 108700023372 Glycosyltransferases Proteins 0.000 description 2
- 239000007995 HEPES buffer Substances 0.000 description 2
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 2
- 102000009617 Inorganic Pyrophosphatase Human genes 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 2
- OVRNDRQMDRJTHS-RTRLPJTCSA-N N-acetyl-D-glucosamine Chemical compound CC(=O)N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-RTRLPJTCSA-N 0.000 description 2
- OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical group CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 description 2
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 2
- LCTONWCANYUPML-UHFFFAOYSA-N Pyruvic acid Chemical group CC(=O)C(O)=O LCTONWCANYUPML-UHFFFAOYSA-N 0.000 description 2
- 108010058532 UTP-hexose-1-phosphate uridylyltransferase Proteins 0.000 description 2
- 102000006321 UTP-hexose-1-phosphate uridylyltransferase Human genes 0.000 description 2
- 125000003275 alpha amino acid group Chemical group 0.000 description 2
- DRTQHJPVMGBUCF-PSQAKQOGSA-N beta-L-uridine Natural products O[C@H]1[C@@H](O)[C@H](CO)O[C@@H]1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-PSQAKQOGSA-N 0.000 description 2
- 150000001793 charged compounds Chemical class 0.000 description 2
- 235000021310 complex sugar Nutrition 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000001177 diphosphate Substances 0.000 description 2
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 2
- 229940027941 immunoglobulin g Drugs 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 239000011591 potassium Substances 0.000 description 2
- 229910052700 potassium Inorganic materials 0.000 description 2
- 239000001103 potassium chloride Substances 0.000 description 2
- 235000011164 potassium chloride Nutrition 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 230000002285 radioactive effect Effects 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- 238000006276 transfer reaction Methods 0.000 description 2
- DRTQHJPVMGBUCF-UHFFFAOYSA-N uracil arabinoside Natural products OC1C(O)C(CO)OC1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-UHFFFAOYSA-N 0.000 description 2
- 229940045145 uridine Drugs 0.000 description 2
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 description 1
- 102100027050 Inorganic pyrophosphatase Human genes 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 102000009097 Phosphorylases Human genes 0.000 description 1
- 108010073135 Phosphorylases Proteins 0.000 description 1
- 108010009413 Pyrophosphatases Proteins 0.000 description 1
- 102000009609 Pyrophosphatases Human genes 0.000 description 1
- LEHOTFFKMJEONL-UHFFFAOYSA-N Uric Acid Chemical compound N1C(=O)NC(=O)C2=C1NC(=O)N2 LEHOTFFKMJEONL-UHFFFAOYSA-N 0.000 description 1
- TVWHNULVHGKJHS-UHFFFAOYSA-N Uric acid Natural products N1C(=O)NC(=O)C2NC(=O)NC21 TVWHNULVHGKJHS-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 229960001456 adenosine triphosphate Drugs 0.000 description 1
- HXXFSFRBOHSIMQ-VFUOTHLCSA-N alpha-D-glucose 1-phosphate Chemical compound OC[C@H]1O[C@H](OP(O)(O)=O)[C@H](O)[C@@H](O)[C@@H]1O HXXFSFRBOHSIMQ-VFUOTHLCSA-N 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000030609 dephosphorylation Effects 0.000 description 1
- XPPKVPWEQAFLFU-UHFFFAOYSA-N diphosphoric acid Chemical compound OP(O)(=O)OP(O)(O)=O XPPKVPWEQAFLFU-UHFFFAOYSA-N 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 229950010772 glucose-1-phosphate Drugs 0.000 description 1
- 150000008131 glucosides Chemical class 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000005040 ion trap Methods 0.000 description 1
- 230000000155 isotopic effect Effects 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 125000000311 mannosyl group Chemical group C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 238000001819 mass spectrum Methods 0.000 description 1
- 238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 1
- 229950006780 n-acetylglucosamine Drugs 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000002250 progressing effect Effects 0.000 description 1
- 229940107700 pyruvic acid Drugs 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 238000005924 transacylation reaction Methods 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 229940116269 uric acid Drugs 0.000 description 1
Images
Landscapes
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Other Investigation Or Analysis Of Materials By Electrical Means (AREA)
Abstract
【解決手段】構造異性体を有し得る解析すべき糖鎖試料の一部の糖を同位体標識し、得られた同位体標識糖鎖の質量分析を行う、糖鎖構造解析手法。前記解析すべき糖鎖試料が分枝糖鎖を有し、前記分枝糖鎖が互いに同じ糖鎖配列を有することが好ましい。また、前記分枝糖鎖の末端糖残基を13Cを用いて同位体標識することが好ましい。
【選択図】図3
Description
これに類似の方法が、以前からタンパク質・ペプチドのアミノ酸配列を推定するために用いられている。すなわち、分子イオンピークとペプチド結合部位で開裂したプロダクトイオンピークとの質量数から、ペプチドを構成するアミノ酸の種類及びアミノ酸配列を推定するDe Novoシーケンス法として広く知られている。
そこで本発明の目的は、分枝構造などを有する糖鎖を構造異性体として識別することができる、糖鎖構造解析手法を提供することにある。
本発明は、以下の発明を含む。
(1)構造異性体を有し得る解析すべき糖鎖試料の一部の糖残基を同位体標識し、得られた同位体標識糖鎖の質量分析を行う、糖鎖構造解析手法。
(3)前記解析すべき糖鎖試料が複数の分枝糖鎖を有し、前記分枝糖鎖が互いに同じ糖鎖配列を有する、(2)に記載の糖鎖構造解析手法。
(4)前記分枝糖鎖の末端糖残基を同位体標識する(2)又は(3)に記載の糖鎖構造解析手法。
(6)(1)〜(5)のいずれかに記載の糖鎖構造解析手法を用いて得られた情報を含むデータベース。
本調製法においては、このような標識糖鎖を合成するための原料として、目的の糖鎖の特定の分枝における標識糖残基の位置に糖残基が存在しない構造を持つ前駆体糖鎖を用いる。なお、本明細書では、目的の標識糖鎖においては標識糖残基を有する分枝、原料の前駆体糖鎖においては標識糖残基が導入されるべき分枝を、特定の分枝と表記する。
PA化糖鎖(III)を、20mM KCl及び5mM MgCl2を含む100mM HEPES緩衝液(pH7.4)に溶解して2pmol/μlとした溶液50μlをチューブに入れ、15mM ATP、22mM [u-13C6]Gal、及び2mU/μlのガラクトキナーゼを加え、37℃で30分反応を行った。その後、13mM UDP-Glc・Na2、0.3mU/μlガラクトース−1−ホスフェートウリジルトランスフェラーゼを加え、37℃、4時間反応を行った。その後、5mM MnCl2、1mU/μlガラクトシルトランスフェラーゼ、30mMホスホエノールピルビン酸カリウム、20mU/μlピルビン酸キナーゼ、3mU/μl無機ピロホスファターゼ、及び1.5mU/μl UDP-Glcホスホリラーゼを加え、さらに、37℃で3日間反応を行った。
Claims (6)
- 構造異性体を有し得る解析すべき糖鎖試料の一部の糖残基を同位体標識し、得られた同位体標識糖鎖の質量分析を行う、糖鎖構造解析手法。
- 前記解析すべき糖鎖試料が分枝糖鎖を有する、請求項1に記載の糖鎖構造解析手法。
- 前記解析すべき糖鎖試料が複数の分枝糖鎖を有し、前記分枝糖鎖が互いに同じ糖鎖配列を有する、請求項2に記載の糖鎖構造解析手法。
- 前記分枝糖鎖の末端糖残基を同位体標識する、請求項2又は3に記載の糖鎖構造解析手法。
- 構造異性体を有しうる糖鎖試料の一部の糖残基が同位体標識された糖鎖を質量分析装置の較正試料として用いる、請求項1〜4のいずれか1項に記載の糖鎖構造解析手法。
- 請求項1〜5のいずれか1項に記載の糖鎖構造解析手法を用いて得られた情報を含むデータベース。
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2004028324A JP4483320B2 (ja) | 2004-02-04 | 2004-02-04 | 糖鎖構造解析手法 |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2004028324A JP4483320B2 (ja) | 2004-02-04 | 2004-02-04 | 糖鎖構造解析手法 |
Publications (2)
Publication Number | Publication Date |
---|---|
JP2005221328A true JP2005221328A (ja) | 2005-08-18 |
JP4483320B2 JP4483320B2 (ja) | 2010-06-16 |
Family
ID=34997086
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2004028324A Expired - Lifetime JP4483320B2 (ja) | 2004-02-04 | 2004-02-04 | 糖鎖構造解析手法 |
Country Status (1)
Country | Link |
---|---|
JP (1) | JP4483320B2 (ja) |
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2007292690A (ja) * | 2006-04-27 | 2007-11-08 | Noguchi Inst | 糖鎖異性体を分離同定する質量分析法 |
JP2013002967A (ja) * | 2011-06-16 | 2013-01-07 | Shimadzu Corp | 質量分析データ表示装置及び質量分析データ表示プログラム |
US20150187553A1 (en) * | 2013-12-26 | 2015-07-02 | Shimadzu Corporation | Mass spectrometry data display device and mass spectrometry data display program |
CN108700551A (zh) * | 2016-02-22 | 2018-10-23 | 株式会社岛津制作所 | 唾液酸糖链解析方法 |
-
2004
- 2004-02-04 JP JP2004028324A patent/JP4483320B2/ja not_active Expired - Lifetime
Cited By (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2007292690A (ja) * | 2006-04-27 | 2007-11-08 | Noguchi Inst | 糖鎖異性体を分離同定する質量分析法 |
JP2013002967A (ja) * | 2011-06-16 | 2013-01-07 | Shimadzu Corp | 質量分析データ表示装置及び質量分析データ表示プログラム |
US20150187553A1 (en) * | 2013-12-26 | 2015-07-02 | Shimadzu Corporation | Mass spectrometry data display device and mass spectrometry data display program |
US9666421B2 (en) * | 2013-12-26 | 2017-05-30 | Shimadzu Corporation | Mass spectrometry data display device and mass spectrometry data display program |
CN108700551A (zh) * | 2016-02-22 | 2018-10-23 | 株式会社岛津制作所 | 唾液酸糖链解析方法 |
CN108700551B (zh) * | 2016-02-22 | 2021-12-03 | 株式会社岛津制作所 | 唾液酸糖链解析方法 |
Also Published As
Publication number | Publication date |
---|---|
JP4483320B2 (ja) | 2010-06-16 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Gray et al. | Advancing solutions to the carbohydrate sequencing challenge | |
Ma et al. | O-GlcNAc profiling: from proteins to proteomes | |
Leymarie et al. | Effective use of mass spectrometry for glycan and glycopeptide structural analysis | |
Merry et al. | Recovery of intact 2-aminobenzamide-labeled O-glycans released from glycoproteins by hydrazinolysis | |
Nishimura | Toward automated glycan analysis | |
US10001488B2 (en) | Synthesis and use of isotopically-labelled glycans | |
Blank et al. | High-throughput mass finger printing and Lewis blood group assignment of human milk oligosaccharides | |
Wang et al. | Quantitative O-glycomics based on improvement of the one-pot method for nonreductive O-glycan release and simultaneous stable isotope labeling with 1-(d0/d5) phenyl-3-methyl-5-pyrazolone followed by mass spectrometric analysis | |
Maszczak-Seneczko et al. | Comparative analysis of involvement of UGT1 and UGT2 splice variants of UDP-galactose transporter in glycosylation of macromolecules in MDCK and CHO cell lines | |
Conway et al. | Functional analysis of anomeric sugar kinases | |
JP4483320B2 (ja) | 糖鎖構造解析手法 | |
Prien et al. | Differentiating N-linked glycan structural isomers in metastatic and nonmetastatic tumor cells using sequential mass spectrometry | |
Voglmeir et al. | Enzymatic glycosylations on arrays | |
Karlsson et al. | Next generation O-linked glycomics | |
US20100221763A1 (en) | Specific Acceptors for Transferases to Saccharides and Method for Obtaining and Using Same | |
Ito et al. | Strategy for the fine characterization of glycosyltransferase specificity using isotopomer assembly | |
JP2005218336A (ja) | 糖鎖の選択的末端糖残基同位体標識法 | |
Péanne et al. | Assessing ER and Golgi N-glycosylation process using metabolic labeling in mammalian cultured cells | |
US20060183155A1 (en) | Compound libraries by glycotransferases and a method of preparing the same | |
JP4808542B2 (ja) | 糖鎖異性体を分離同定する質量分析法 | |
Wong et al. | Highlights in Chemical Glycobiology | |
Caputi et al. | A one-pot enzymatic approach to the O-fluoroglucoside of N-methylanthranilate | |
van Outersterp et al. | Distinguishing Oligosaccharide Isomers Using Far-Infrared Ion Spectroscopy: Identification of Biomarkers for Inborn Errors of Metabolism | |
WO2006043405A1 (ja) | 糖鎖構造解析方法 | |
Kinoshita et al. | Structural characterization of multibranched oligosaccharides from seal milk by a combination of off-line high-performance liquid chromatography–matrix-assisted laser desorption/ionization–time-of-flight mass spectrometry and sequential exoglycosidase digestion |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20060605 |
|
A977 | Report on retrieval |
Free format text: JAPANESE INTERMEDIATE CODE: A971007 Effective date: 20080909 |
|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20090908 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20091109 |
|
TRDD | Decision of grant or rejection written | ||
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20100302 |
|
A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20100315 |
|
R151 | Written notification of patent or utility model registration |
Ref document number: 4483320 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R151 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130402 Year of fee payment: 3 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130402 Year of fee payment: 3 |
|
FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20140402 Year of fee payment: 4 |
|
EXPY | Cancellation because of completion of term |