In vitro induction and proteomics characterisation of a uranyl-protein interaction network in bovine serum - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Metallomics Année : 2015

In vitro induction and proteomics characterisation of a uranyl-protein interaction network in bovine serum

Ł. Szyrwiel
  • Fonction : Auteur
V. Liauchuk
  • Fonction : Auteur
L. Chavatte

Résumé

Uranyl ions (UO2 2+) were shown to interact with a number of foetal serum proteins, leading to the formation of a complex that could be isolated by ultracentrifugation. The molecular weight of the complex was estimated based on size-exclusion chromatography as 650 000 Da. Online ICP AES detection indicated that UO2 2+ in the complex co-eluted with minor amounts of calcium and phosphorous, but not with magnesium. A 1D gel electrophoresis of the U-complex produced more than 10 bands of similar intensity compared with only 2-3 intense bands corresponding to the main serum proteins in the control serum, indicative of the specific interaction of UO2 2+ with minor proteins. A proteomics approach allowed for the identification of 74 proteins in the complex. Analysis of the protein-protein interaction network in the UO2 2+ complex identified 32 proteins responsible for protein-protein complex formation and 34 with demonstrated ion-binding function, suggesting that UO2 2+ stimulates the formation of protein functional networks rather than using a particular molecule as its target. © 2015 The Royal Society of Chemistry.

Dates et versions

hal-01505923 , version 1 (11-04-2017)

Identifiants

Citer

Ł. Szyrwiel, V. Liauchuk, L. Chavatte, Ryszard Lobinski. In vitro induction and proteomics characterisation of a uranyl-protein interaction network in bovine serum. Metallomics, 2015, 7 (12), pp.1604--1611. ⟨10.1039/c5mt00207a⟩. ⟨hal-01505923⟩
59 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More