{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,26]],"date-time":"2025-10-26T16:05:50Z","timestamp":1761494750140,"version":"build-2065373602"},"reference-count":28,"publisher":"Wiley","issue":"23","license":[{"start":{"date-parts":[[2009,11,9]],"date-time":"2009-11-09T00:00:00Z","timestamp":1257724800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Rapid Comm Mass Spectrometry"],"published-print":{"date-parts":[[2009,12,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Homocysteinylation is a post\u2010translational protein modification which involves homocysteine\u2010thiolactone and may be responsible for many pathophysiological changes secondary to hyperhomocysteinemia. Therefore, methods to measure protein homocysteinylation in intact biological samples are required. We tested whether matrix assisted\u2010laser\/desorption ionization mass spectrometry (MALDI\u2010MS) can detect time\u2010 and dose\u2010dependent changes in\n                    <jats:italic>in vitro<\/jats:italic>\n                    homocysteine\u2010thiolactone binding to human serum albumin. We have compared this method with a\n                    <jats:sup>35<\/jats:sup>\n                    S\u2010thiolactone radioactive binding assay. Incubations with and without dithiothreitol allowed measurement of the amide\u2010linked and disulfide\u2010linked thiolactone\u2010protein adducts, respectively. A good correspondence in time\u2010 and dose\u2010dependent protein\u2010thiolactone formation was observed between the two methods. A maximum of 9 to 12 thiolactone residues were bound to each albumin molecule. The\n                    <jats:sup>35<\/jats:sup>\n                    S\u2010thiolactone bound albumin tightly, particularly at the lowest concentrations, with \u224870% of the binding amide\u2010linked. Although the results of the two methods were rather similar, the radioactive method appears to be more sensitive than the MALDI\u2010MS technique. Copyright \u00a9 2009 John Wiley &amp; Sons, Ltd.\n                  <\/jats:p>","DOI":"10.1002\/rcm.4290","type":"journal-article","created":{"date-parts":[[2009,11,9]],"date-time":"2009-11-09T04:56:55Z","timestamp":1257742615000},"page":"3837-3842","source":"Crossref","is-referenced-by-count":4,"title":["Kinetics of albumin homocysteinylation measured with matrix\u2010assisted laser\/desorption ionization mass spectrometry versus with a radioactive tracer"],"prefix":"10.1002","volume":"23","author":[{"given":"Elisabetta","family":"Callegher","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roberta","family":"Seraglia","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Monica","family":"Vettore","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lucia","family":"Puricelli","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Renato","family":"Millioni","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paolo","family":"Tessari","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2009,11,9]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1161\/01.CIR.79.6.1180"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1161\/01.ATV.0000219688.43572.75"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1160\/TH04-08-0493"},{"key":"e_1_2_7_5_2","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1055\/s-0038-1657580","volume":"78","author":"Boers GH","year":"1997","journal-title":"Thromb. 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