{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,17]],"date-time":"2026-03-17T07:08:28Z","timestamp":1773731308909,"version":"3.50.1"},"reference-count":24,"publisher":"Wiley","issue":"16","license":[{"start":{"date-parts":[[2013,7,24]],"date-time":"2013-07-24T00:00:00Z","timestamp":1374624000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Electrophoresis"],"published-print":{"date-parts":[[2013,8]]},"abstract":"<jats:p>The identification of sialylated <jats:styled-content style=\"fixed-case\">T<\/jats:styled-content>homsen\u2013Friedenreich antigens in proteins poses much interest in the context of cancer research. <jats:styled-content style=\"fixed-case\">MALDI<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">TOF<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">MS<\/jats:styled-content> is a powerful technique for this purpose; still it shows considerable low sensitivity for sialylated molecules due to in\u2010source and metastable decomposition. Herein, we report a target\u2010driven strategy to identify these antigens in minute amounts of glycoproteins isolated in polyacrylamide gels. The glycans were recovered from gel spots by reductive <jats:italic>\u03b2<\/jats:italic>\u2010elimination, permethylated and analyzed by nano\u2010<jats:styled-content style=\"fixed-case\">LC<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">MALDI<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">TOF<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">MS<\/jats:styled-content>. A computational algorithm was developed to filter spectral noise and enhance\/isolate the signals of interest. Sialylated antigens were identified in minute amounts of fetuin (0.1 \u03bcg) and plasminogen (1.0 \u03bcg) by this approach.<jats:styled-content style=\"fixed-case\">MS<\/jats:styled-content> assignments were further validated by enzymatic methods. This methodology allowed a fivefold decrease in the current <jats:styled-content style=\"fixed-case\">LOD<\/jats:styled-content> of fetuin sialylated <jats:italic>O<\/jats:italic>\u2010glycans by <jats:styled-content style=\"fixed-case\">MALDI<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">TOF<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">MS<\/jats:styled-content>.<\/jats:p>","DOI":"10.1002\/elps.201300148","type":"journal-article","created":{"date-parts":[[2013,6,17]],"date-time":"2013-06-17T15:44:14Z","timestamp":1371483854000},"page":"2337-2341","source":"Crossref","is-referenced-by-count":12,"title":["Challenging the limits of detection of sialylated <scp>T<\/scp>homsen\u2013<scp>F<\/scp>riedenreich antigens by in\u2010gel deglycosylation and nano\u2010<scp>LC<\/scp>\u2010<scp>MALDI<\/scp>\u2010<scp>TOF<\/scp>\u2010<scp>MS<\/scp>"],"prefix":"10.1002","volume":"34","author":[{"given":"Andreia","family":"Almeida","sequence":"first","affiliation":[{"name":"Department of Chemistry, Mass Spectrometry Centre QOPNA University of Aveiro Campus de Santiago  Aveiro Portugal"}]},{"given":"Jos\u00e9 A.","family":"Ferreira","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Mass Spectrometry Centre QOPNA University of Aveiro Campus de Santiago  Aveiro Portugal"},{"name":"Experimental Pathology and Therapeutics Group Portuguese Institute for Oncology Porto Portugal"}]},{"given":"Filipe","family":"Teixeira","sequence":"additional","affiliation":[{"name":"REQUIMTE, Department of Chemistry and Biochemistry Faculty of Sciences, University of Porto Portugal"}]},{"given":"Catarina","family":"Gomes","sequence":"additional","affiliation":[{"name":"Institute of Molecular Pathology and Immunology University of Porto (IPATIMUP) Porto Portugal"}]},{"given":"M. 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