{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T00:32:39Z","timestamp":1760920359164,"version":"build-2065373602"},"reference-count":23,"publisher":"Wiley","issue":"22","license":[{"start":{"date-parts":[[2009,11,3]],"date-time":"2009-11-03T00:00:00Z","timestamp":1257206400000},"content-version":"vor","delay-in-days":2,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Separation Science"],"published-print":{"date-parts":[[2009,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Open\u2010tubular CEC (OT\u2010CEC) with a new stationary phase, salophene\u2013lanthanide\u2013Zn<jats:sup>2+<\/jats:sup> complex, has been applied to the separation of tryptic peptides of native BSA and BSA glycated by glucose and ribose. Glycation of proteins (non\u2010enzymatic modification by sugars) significantly affects their properties and it is of great importance from a physiological point of view. Separation of tryptic peptides of glycated BSA by CZE was poor because of their strong adsorption to the bare fused silica capillary. An improved separation of tryptic peptides of both native and glycated BSA was achieved by OT\u2010CEC in the fused silica capillary non\u2010covalently coated with salophene\u2013lanthanide\u2013Zn<jats:sup>2+<\/jats:sup> complex, which suppressed the adsorption of peptides to the capillary and <jats:italic>via<\/jats:italic> specific interactions with some (glyco)peptides enhanced selectivity of the separation. Significant differences have been found in OT\u2010CEC analyses of tryptic hydrolysates of native and glycated BSA. In OT\u2010CEC\u2010UV profile of tryptic peptides of native BSA, 44 peaks could be resolved, whereas a reduced number of 38 peaks were observed in the profile of tryptic peptides of glucose\u2010glycated BSA and only 30 peaks were found in the case of ribose\u2010glycated BSA. The developed OT\u2010CEC can be potentially used for monitoring of protein glycation.<\/jats:p>","DOI":"10.1002\/jssc.200900513","type":"journal-article","created":{"date-parts":[[2009,11,3]],"date-time":"2009-11-03T15:32:16Z","timestamp":1257262336000},"page":"3930-3935","source":"Crossref","is-referenced-by-count":13,"title":["Separation of tryptic peptides of native and glycated BSA using open\u2010tubular CEC with salophene\u2013lanthanide\u2013Zn<sup>2+<\/sup> complex as stationary phase"],"prefix":"10.1002","volume":"32","author":[{"given":"Pavla","family":"Sedl\u00e1kov\u00e1","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adam","family":"Eckhardt","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kate\u0159ina","family":"Lacinov\u00e1","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Statis","family":"Pataridis","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ivan","family":"Mik\u0161\u00edk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Vladim\u00edr","family":"Kr\u00e1l","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"V\u00e1clav","family":"Ka\u0161i\u010dka","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,12,23]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0301-4770(01)80082-8"},{"volume-title":"Capillary Electrochromatography and Pressurized Flow Capillary Electrochromatography: An Introduction","year":"2000","author":"Krull I. 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