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Volumn 346, Issue 1, 2005, Pages 124-131

Ion-selective enrichment of tyrosine-sulfated peptides from complex protein digests

Author keywords

Affinity purification; Bovine fibrinogen; Ion selectivity; Mass spectrometry; Sulfated peptide; Tyrosine sulfation

Indexed keywords

AMINO ACIDS; ION EXCHANGE RESINS; MAMMALS; MASS SPECTROMETRY; MOLAR RATIO; PEPTIDES; SULFUR COMPOUNDS;

EID: 26844525759     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.06.047     Document Type: Article
Times cited : (23)

References (26)
  • 1
    • 0041589205 scopus 로고    scopus 로고
    • The biology and enzymology of protein tyrosine O-sulfation
    • K.L. Moore The biology and enzymology of protein tyrosine O-sulfation J. Biol. Chem. 278 2003 24243 24246
    • (2003) J. Biol. Chem. , vol.278 , pp. 24243-24246
    • Moore, K.L.1
  • 2
    • 0023851252 scopus 로고
    • Tyrosine sulfation and the secretory pathway
    • W.B. Huttner Tyrosine sulfation and the secretory pathway Annu. Rev. Physiol. 50 1988 363 376
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 363-376
    • Huttner, W.B.1
  • 4
    • 0014421640 scopus 로고
    • Structure of porcine cholecystokinin-pancreozymin: I. Cleavage with thrombin and with trypsin
    • V. Mutt, and J.E. Jorpes Structure of porcine cholecystokinin- pancreozymin: I. Cleavage with thrombin and with trypsin Eur. J. Biochem. 6 1968 156 162
    • (1968) Eur. J. Biochem. , vol.6 , pp. 156-162
    • Mutt, V.1    Jorpes, J.E.2
  • 5
    • 0014277985 scopus 로고
    • Isolation and amino acid sequence of caerulein, the active decapeptide of the skin of Hyla caerulea
    • A. Anastasi, V. Erspamer, and R. Endean Isolation and amino acid sequence of caerulein, the active decapeptide of the skin of Hyla caerulea Arch. Biochem. Biophys. 125 1968 57 68
    • (1968) Arch. Biochem. Biophys. , vol.125 , pp. 57-68
    • Anastasi, A.1    Erspamer, V.2    Endean, R.3
  • 6
    • 0025261194 scopus 로고
    • Cionin: A disulfotyrosyl hybrid of cholecystokinin and gastrin from the neural ganglion of the protochordate Ciona intestinalis
    • A.H. Johnsen, and J.F. Rehfeld Cionin: a disulfotyrosyl hybrid of cholecystokinin and gastrin from the neural ganglion of the protochordate Ciona intestinalis J. Biol. Chem. 265 1990 3054 3058
    • (1990) J. Biol. Chem. , vol.265 , pp. 3054-3058
    • Johnsen, A.H.1    Rehfeld, J.F.2
  • 7
    • 0022996473 scopus 로고
    • Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin
    • R.J. Nachman, G.M. Holman, W.F. Haddon, and N. Ling Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin Science 234 1986 71 73
    • (1986) Science , vol.234 , pp. 71-73
    • Nachman, R.J.1    Holman, G.M.2    Haddon, W.F.3    Ling, N.4
  • 10
    • 0029821720 scopus 로고    scopus 로고
    • Phytosulfokine: Sulfated peptides that induce the proliferation of single mesophyll cells of Asparagus officinalis L
    • Y. Matsubayashi, and Y. Sakagami Phytosulfokine: sulfated peptides that induce the proliferation of single mesophyll cells of Asparagus officinalis L Proc. Natl. Acad. Sci. USA 93 1996 7623 7627
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7623-7627
    • Matsubayashi, Y.1    Sakagami, Y.2
  • 11
    • 0034708702 scopus 로고    scopus 로고
    • Existence of a plant tyrosylprotein sulfotransferase: Novel plant enzyme catalyzing tyrosine O-sulfation of preprophytosulfokine variants in vitro
    • H. Hanai, D. Nakayama, H. Yang, Y. Matsubayashi, Y. Hirota, and Y. Sakagami Existence of a plant tyrosylprotein sulfotransferase: novel plant enzyme catalyzing tyrosine O-sulfation of preprophytosulfokine variants in vitro FEBS Lett. 470 2000 97 101
    • (2000) FEBS Lett. , vol.470 , pp. 97-101
    • Hanai, H.1    Nakayama, D.2    Yang, H.3    Matsubayashi, Y.4    Hirota, Y.5    Sakagami, Y.6
  • 12
    • 0022898047 scopus 로고
    • Characterization of sites of tyrosine sulfation in proteins and criteria for predicting their occurrence
    • G. Hortin, R. Folz, J.I. Gordon, and A.W. Strauss Characterization of sites of tyrosine sulfation in proteins and criteria for predicting their occurrence Biochem. Biophys. Res. Commun. 141 1986 326 333
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 326-333
    • Hortin, G.1    Folz, R.2    Gordon, J.I.3    Strauss, A.W.4
  • 13
    • 0036088377 scopus 로고    scopus 로고
    • The Sulfinator: Predicting tyrosine sulfation sites in protein sequences
    • F. Monigatti, E. Gasteiger, A. Bairoch, and E. Jung The Sulfinator: predicting tyrosine sulfation sites in protein sequences Bioinformatics 18 2002 769 770
    • (2002) Bioinformatics , vol.18 , pp. 769-770
    • Monigatti, F.1    Gasteiger, E.2    Bairoch, A.3    Jung, E.4
  • 14
    • 0347683486 scopus 로고    scopus 로고
    • Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry
    • P. Önnerfjord, T.F. Heathfield, and D. Heinegard Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry J. Biol. Chem. 279 2004 26 33
    • (2004) J. Biol. Chem. , vol.279 , pp. 26-33
    • Önnerfjord, P.1    Heathfield, T.F.2    Heinegard, D.3
  • 15
    • 0021118791 scopus 로고
    • Determination and occurrence of tyrosine O-sulfate in proteins
    • W.B. Huttner Determination and occurrence of tyrosine O-sulfate in proteins Methods Enzymol. 107 1984 200 223
    • (1984) Methods Enzymol. , vol.107 , pp. 200-223
    • Huttner, W.B.1
  • 16
    • 4444337337 scopus 로고    scopus 로고
    • Protein tyrosine O-sulfation analysis by exhaustive product ion scanning with minimum collision offset in a NanoESI Q-TOF tandem mass spectrometer
    • M. Salek, S. Costagliola, and W.D. Lehmann Protein tyrosine O-sulfation analysis by exhaustive product ion scanning with minimum collision offset in a NanoESI Q-TOF tandem mass spectrometer Anal. Chem. 76 2004 5136 5142
    • (2004) Anal. Chem. , vol.76 , pp. 5136-5142
    • Salek, M.1    Costagliola, S.2    Lehmann, W.D.3
  • 17
    • 0035673710 scopus 로고    scopus 로고
    • Analysis of sulfated peptides using positive electrospray ionization tandem mass spectrometry
    • J.F. Nemeth-Cawley, S. Karnik, and J.C. Rouse Analysis of sulfated peptides using positive electrospray ionization tandem mass spectrometry J. Mass Spectrom. 36 2001 1301 1311
    • (2001) J. Mass Spectrom. , vol.36 , pp. 1301-1311
    • Nemeth-Cawley, J.F.1    Karnik, S.2    Rouse, J.C.3
  • 18
    • 0023022190 scopus 로고
    • Selective adsorption of phosphoproteins on gel-immobilized ferric chelate
    • G. Muszynska, L. Andersson, and J. Porath Selective adsorption of phosphoproteins on gel-immobilized ferric chelate Biochemistry 25 1986 6850 6853
    • (1986) Biochemistry , vol.25 , pp. 6850-6853
    • Muszynska, G.1    Andersson, L.2    Porath, J.3
  • 19
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • M.C. Posewitz, and P. Tempst Immobilized gallium(III) affinity chromatography of phosphopeptides Anal. Chem. 71 1999 2883 2892
    • (1999) Anal. Chem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 20
    • 26844505594 scopus 로고
    • Aqueous-phase ion solvation and the selectivity of ion exchange resins for monovalent anions
    • S. Subramonian, and D. Clifford Aqueous-phase ion solvation and the selectivity of ion exchange resins for monovalent anions J. Solut. Chem. 18 1989 529 543
    • (1989) J. Solut. Chem. , vol.18 , pp. 529-543
    • Subramonian, S.1    Clifford, D.2
  • 21
    • 0030570746 scopus 로고    scopus 로고
    • Active fragments and analogs of the plant growth factor, phytosulfokine: Structure-activity relationships
    • Y. Matsubayashi, H. Hanai, O. Hara, and Y. Sakagami Active fragments and analogs of the plant growth factor, phytosulfokine: Structure-activity relationships Biochem. Biophys. Res. Commun. 225 1996 209 214
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 209-214
    • Matsubayashi, Y.1    Hanai, H.2    Hara, O.3    Sakagami, Y.4
  • 22
    • 0027322968 scopus 로고
    • 3H)-containing peptides with 9-fluorenylmethyloxycarbonyl (Fmoc)-strategy and its application to the synthesis of cholecystokinin (CCK)-12
    • 3H)- containing peptides with 9-fluorenylmethyloxycarbonyl (Fmoc)-strategy and its application to the synthesis of cholecystokinin (CCK)-12 Chem. Pharm. Bull. 41 1993 376 380
    • (1993) Chem. Pharm. Bull. , vol.41 , pp. 376-380
    • Yagami, T.1    Shiwa, S.2    Futaki, S.3    Kitagawa, K.4
  • 23
    • 0022068293 scopus 로고
    • Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid
    • F. Marcus Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid Int. J. Pept. Proteins Res. 25 1985 542 546
    • (1985) Int. J. Pept. Proteins Res. , vol.25 , pp. 542-546
    • Marcus, F.1
  • 24
    • 72949132269 scopus 로고
    • Carboxy-peptidase B: IV. Purification and characterization of the porcine enzyme
    • J.E. Folk, K.A. Piez, W.R. Carroll, and J.A. Gladner Carboxy-peptidase B: IV. Purification and characterization of the porcine enzyme J. Biol. Chem. 235 1960 2272 2277
    • (1960) J. Biol. Chem. , vol.235 , pp. 2272-2277
    • Folk, J.E.1    Piez, K.A.2    Carroll, W.R.3    Gladner, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.