Characteristics and molecular mechanism of adhesion proteins on reused hemodialysis membranes.
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.
Xu
Xiulin
X
Institute of Medical Device and Food Sciences, University of Shanghai for Science and Technology, Shanghai, China.
Yang
Yujing
Y
Zhu
Naishuo
N
D000327:Adsorption; D024342:Amino Acids, Acidic; D001798:Blood Proteins / Q000032:analysis*; D003176:Complement C3; D006801:Humans; D037102:Lectins; D050606:Mannose-Binding Protein-Associated Serine Proteases; D008567:Membranes, Artificial; D011108:Polymers; D011485:Protein Binding; D006435:Renal Dialysis / Q000295:instrumentation*; D012709:Serum Albumin; D055672:Static Electricity; D013450:Sulfones; D000097604:Ficolins
D024342:Amino Acids, Acidic; D001798:Blood Proteins; D003176:Complement C3; D037102:Lectins; D050606:Mannose-Binding Protein-Associated Serine Proteases; D008567:Membranes, Artificial; D011108:Polymers; D012709:Serum Albumin; D013450:Sulfones; D000097604:Ficolins; C017662:polysulfone P 1700; C084067:MASP1 protein, human