Publisher: Karger
E-ISSN: 1421-9735|27|4|321-329
ISSN: 0253-5068
Source: Blood Purification, Vol.27, Iss.4, 2009-03, pp. : 321-329
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
In order to study the mechanism of protein adhesion on the Fresenius F6 polysulfone membrane dialyzer, two-dimensional gel electrophoresis, LC-ESI-MS/MS and bioinformatics methods were used to analyze the protein which adhered to the dialyzer membrane. Six of the adhered proteins account for more than 50% of the total 179 proteins, i.e. ficolin precursor, complement C3 precursor, 3 variants of MASP1 and albumin. The results also showed that easily adhered proteins have a greater percentage of acidic amino acids (p < 0.01). The isoelectric point of the 20 proteins with the most deposits is 6.2 ± 1.08, which is obviously lower than of those with the least deposits (7.56 ± 1.36, p < 0.01). The dipole moment of a polysulfone membrane molecule has a tendency to absorb molecules with a negative charge. These results are of significance in understanding and improving membrane protein interactions.
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