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In vitro induction and proteomics characterisation of a uranyl–protein interaction network in bovine serum
- Source :
- Metallomics, Metallomics, Royal Society of Chemistry, 2015, 7 (12), pp.1604--1611. ⟨10.1039/c5mt00207a⟩
- Publication Year :
- 2015
- Publisher :
- Oxford University Press (OUP), 2015.
-
Abstract
- International audience; 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.
- Subjects :
- Proteomics
Biophysics
chemistry.chemical_element
Plasma protein binding
Calcium
Biochemistry
Biomaterials
chemistry.chemical_compound
[CHIM.ANAL]Chemical Sciences/Analytical chemistry
Protein Interaction Mapping
Animals
[CHIM]Chemical Sciences
Protein Interaction Maps
Bovine serum albumin
Gel electrophoresis
Chromatography
biology
Metals and Alloys
Blood Proteins
Uranyl
Uranium Compounds
Blood proteins
chemistry
Chemistry (miscellaneous)
biology.protein
Cattle
Ultracentrifuge
Protein Binding
Subjects
Details
- ISSN :
- 1756591X and 17565901
- Volume :
- 7
- Database :
- OpenAIRE
- Journal :
- Metallomics
- Accession number :
- edsair.doi.dedup.....1506ccb42e4f63bea4f5ae314f07cc22
- Full Text :
- https://doi.org/10.1039/c5mt00207a