Characteristics and Molecular Mechanism of Adhesion Proteins on Reused Hemodialysis Membranes

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

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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.