Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Evaluation of desorption of proteins adsorbed to hydrophilic surfaces by two-dimensional electrophoresis
Autore:
Lind, K; Kresse, M; Muller, RH;
Indirizzi:
Free Univ Berlin, Dept Pharmaceut Technol, D-12169 Berlin, Germany Free Univ Berlin Berlin Germany D-12169 Technol, D-12169 Berlin, Germany Inst Diagnost Res, Berlin, Germany Inst Diagnost Res Berlin GermanyInst Diagnost Res, Berlin, Germany Schering AG, D-1000 Berlin, Germany Schering AG Berlin Germany D-1000Schering AG, D-1000 Berlin, Germany
Titolo Testata:
PROTEOMICS
fascicolo: 9, volume: 1, anno: 2001,
pagine: 1059 - 1066
SICI:
1615-9853(200109)1:9<1059:EODOPA>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYACRYLAMIDE-GEL ELECTROPHORESIS; ADSORPTION PATTERNS; 2-DIMENSIONAL ELECTROPHORESIS; SAMPLE PREPARATION; PLASMA; RESOLUTION; ESTABLISHMENT; PARTICLES;
Keywords:
plasma protein adsorption; two-dimensional electrophoresis; protein quantification; desorption; hydrophilic surfaces;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Muller, RH Free Univ Berlin, Dept Pharmaceut Technol, Kelchstr 31, D-12169Berlin, Germany Free Univ Berlin Kelchstr 31 Berlin Germany D-12169 n, Germany
Citazione:
K. Lind et al., "Evaluation of desorption of proteins adsorbed to hydrophilic surfaces by two-dimensional electrophoresis", PROTEOMICS, 1(9), 2001, pp. 1059-1066

Abstract

The evaluation of the plasma protein adsorption patterns of superparamagnetic iron oxide (SPIO) particles is of high interest concerning their in vivo fate and is carried out by two-dimensional electrophoresis (2-DE). The sample preparation is of great importance, especially the removal of the adsorbed proteins (desorption) from the particle surface for subsequent analysis by 2-DE. The removal is carried out by a desorption solution. In this study, negatively and positively charged SPIO model particles were under investigation concerning the desorption of proteins adsorbed on their surfaces. Firstly, the desorption process was determined quantitatively using the Bradford protein assay. Secondly, the removable or nonremovable protein species, from particles surface were under investigation by 2-DE. Looking at the desorption in a quantitative manner with the Bradford assay, the desorptionefficacy from negatively charged particles was about 90%. In the case of the positively charged particles, the desorption efficacy seemed to be reduced, approximately 34% of the proteins remained on the surface. Comparing the protein patterns of the particles evaluated by 2-DE in the desorption solution and the proteins remaining on the particles, they confirmed the results from the protein quantification. After desorption, the IgG gamma -chainswere found to be the dominant protein fraction remaining on the negativelycharged particles. On the positively charged particles, many more protein species were found after desorption. The more basic the protein fragments, the more ineffective was the desorption from the positively charged model particle, and vice versa. Nevertheless, all protein spots were found qualitatively in the desorption solution, especially when the desorption solutionsstill containing the particles were used for the 2-DE analysis. In conclusion, 2-DE could be confirmed as the "gold standard" for determining the plasma protein adsorption patterns of nanoparticulate systems.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 09:20:43