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Charge density ribonuclease adsorption

Fig. 6. Plateau-values, I"P1 /mg m 2, of adsorption isotherms of lysozyme (LSZ), ribonuclease (RNase), a -lactalbumin (aLA), calcium-depleted (X -lactalbumin (aLA(-Ca )) and bovine serum albumin (BSA) on hydrophobic polystyrene (PS) and hydrophilic hematite (a — Fe203) and silica (Si02) surfaces. An indication of the charge density of the surface is given by the zeta-potential, C, and of the proteins by + and signs. Ionic strength 0.05 M T = 25°C. (Derived from Currie et al. 2003). Fig. 6. Plateau-values, I"P1 /mg m 2, of adsorption isotherms of lysozyme (LSZ), ribonuclease (RNase), a -lactalbumin (aLA), calcium-depleted (X -lactalbumin (aLA(-Ca )) and bovine serum albumin (BSA) on hydrophobic polystyrene (PS) and hydrophilic hematite (a — Fe203) and silica (Si02) surfaces. An indication of the charge density of the surface is given by the zeta-potential, C, and of the proteins by + and signs. Ionic strength 0.05 M T = 25°C. (Derived from Currie et al. 2003).
The surface adsorption behavior of lysozyme with an anodic end potential of 1.0 V over the temperature range 273-343 K (Fig. 21) showed a steady increase of surface charge density with temperature. Similar results were obtained with ribonuclease A, as shown in Fig. 22. Negligible... [Pg.386]

See other pages where Charge density ribonuclease adsorption is mentioned: [Pg.148]    [Pg.356]    [Pg.364]    [Pg.368]    [Pg.122]    [Pg.276]   
See also in sourсe #XX -- [ Pg.369 ]



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