Kinetics of albumin homocysteinylation measured with matrix-assisted laser/desorption ionization mass spectrometry versus with a radioactive tracer (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Kinetics of albumin homocysteinylation measured with matrix-assisted laser/desorption ionization mass spectrometry versus with a radioactive tracer (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

Alternative label

• Callegher, E,; Seraglia, R.; Vettore, M.; Puricelli, L.; Millioni, R.; Tessari, P. (2009)
  Kinetics of albumin homocysteinylation measured with matrix-assisted laser/desorption ionization mass spectrometry versus with a radioactive tracer
  in RCM. Rapid communications in mass spectrometry
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Callegher, E,; Seraglia, R.; Vettore, M.; Puricelli, L.; Millioni, R.; Tessari, P. (literal)

Pagina inizio

• 3837 (literal)

Pagina fine

• 3842 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 23 (literal)

Rivista

• RCM. Rapid communications in mass spectrometry (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note

• DOI: 10.1002/rcm.4290 (literal)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Kinetics of albumin homocysteinylation measured with matrix-assisted laser/desorption ionization mass spectrometry versus with a radioactive tracer (literal)

Abstract

• Homocysteinylation is a post-translational protein modification which involves homocysteine-thiolactone 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-laser/desorption ionization mass spectrometry (MALDI-MS) can detect time- and dose-dependent changes in in vitro homocysteine-thiolactone binding to human serum albumin. We have compared this method with a S-35-thiolactone radioactive binding assay. Incubations with and without dithiothreitol allowed measurement of the amide-linked and disulfide-linked thiolactone-protein adducts, respectively. A good correspondence in time- and dose-dependent protein-thiolactone formation was observed between the two methods. A maximum of 9 to 12 thiolactone residues were bound to each albumin molecule. The S-35-thiolactone bound albumin tightly, particularly at the lowest concentrations, with approximate to 70% of the binding amide-linked. Although the results of the two methods were rather similar, the radioactive method appears to be more sensitive than the MALDI-MS technique. Copyright (C) 2009 John Wiley & Sons, Ltd. (literal)

Prodotto di

• Identificazione biomarcatori proteici per diabete, nefropatie e tumori mediante spettrometria di massa (PM.P06.008.001) (Modulo)
• Institute of molecular science and technologies (ISTM) (Istituto)

Autore CNR

• ROBERTA SERAGLIA (Persona)

Incoming links:

Prodotto

• Institute of molecular science and technologies (ISTM) (Istituto)
• Identificazione biomarcatori proteici per diabete, nefropatie e tumori mediante spettrometria di massa (PM.P06.008.001) (Modulo)

Autore CNR di

• ROBERTA SERAGLIA (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• RCM. Rapid communications in mass spectrometry (Rivista)