1991
DOI: 10.1002/jhrc.1240140117
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Impact of wall modifications on protein elution in high performance capillary zone electrophoresis

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Cited by 41 publications
(8 citation statements)
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“…However, Eq. (1) points to another mechanism, namely viscosity increase in the electric double layer close to the wall, e.g., due to a voluminous coating [13]. To enhance this effect, the immobilized polymer has to be solvated by the solvent.…”
Section: Introductionmentioning
confidence: 98%
See 1 more Smart Citation
“…However, Eq. (1) points to another mechanism, namely viscosity increase in the electric double layer close to the wall, e.g., due to a voluminous coating [13]. To enhance this effect, the immobilized polymer has to be solvated by the solvent.…”
Section: Introductionmentioning
confidence: 98%
“…Some are based on silanization of surface silanol groups with alkyl silanes [14][15][16][17], others involve derivatization with anchor groups for a consecutive polymerization or polymer immobilization step. Anchor groups can be glycidsilanes for polyethylene glycol coatings [18], aminosilanes for maltopolysaccharides via reductive amination [19], or for protein binding after glutardialdehyde modification [13] as well as methacryloyltrimethoxysilane for polyacrylamide [20], and vinylsilanes for polymerization of acrylamide [21,22] or vinyl acetate to prepare PVA coatings [23,24]. A noncovalent immobilization of PVA was published by Gilges et al [25].…”
Section: Introductionmentioning
confidence: 99%
“…The use of polymeric coatings has led to high efficiency and reproducible protein separations preventing the surface adsorptions. Polymers ranging from highly hydrophobic to highly hydrophilic were used for this purpose to obtain efficient separations of proteins in CE [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16].…”
Section: Introductionmentioning
confidence: 99%
“…Four different approaches have been reported and involve, briefly, (i) elimination of the interaction by adjusting the pH of the buffer to such a value that the silanol groups are non-charged [1]; (ii) adjusting the pH of the buffer of such a value that the charges of the silanol groups and protein have the same sign [2,3]; (iii) dynamic modification of the surface by neutral and cationic additives in the buffer [4][5][6][7][8][9]; and (iv) chemical modification using covalent bonding of the fusedsilica surface [10][11][12][13][14][15][16][17][18].…”
Section: Introductionmentioning
confidence: 99%