1985
DOI: 10.1016/0166-6622(85)80258-4
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Adsorption of human albumin and fibrinogen onto heparin-like materials I. Adsorption isotherms

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Cited by 32 publications
(10 citation statements)
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“…On positively charged nanogels of pure chitosan, the interface consists of fully hydrated loose polysaccharide chains25 whereas, for the negative ones, the interface bears hydrophobic patches arising from the charge neutralization between chitosan and chondroitin sulfate. The data from the isotherms were fitted with Freundlich's model44 and our results are in favor of a diffusion of the proteins within the bulk of the colloid as no protein/protein interactions could be evidenced. Since these data were obtained in the presence of electrolyte (150 × 10 −3 M ), the counter‐ions release effect was ruled out; hence hydrogen bonds and hydrophobic interactions played a significant role in the binding mechanism.…”
Section: Resultsmentioning
confidence: 88%
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“…On positively charged nanogels of pure chitosan, the interface consists of fully hydrated loose polysaccharide chains25 whereas, for the negative ones, the interface bears hydrophobic patches arising from the charge neutralization between chitosan and chondroitin sulfate. The data from the isotherms were fitted with Freundlich's model44 and our results are in favor of a diffusion of the proteins within the bulk of the colloid as no protein/protein interactions could be evidenced. Since these data were obtained in the presence of electrolyte (150 × 10 −3 M ), the counter‐ions release effect was ruled out; hence hydrogen bonds and hydrophobic interactions played a significant role in the binding mechanism.…”
Section: Resultsmentioning
confidence: 88%
“…No saturation of the colloid was observed, in the concentration range investigated. Fitting our data with the Freundlich model:44 (where Γ is the sorption capacity, c the concentration of free protein at equilibrium, K the constant equilibrium and n is the Freundlich exponent), it comes that the Freundlich exponent is close to 1, throughout the experimental concentration range, meaning that there is only one sorption mode of the antibody, depending on the protein/colloid interactions. Therefore, this high sorption capacity is neither due to potentially aggregated proteins at high IgG concentration, nor to a multi layer sorption, which would have required the existence of various protein–protein interactions.…”
Section: Resultsmentioning
confidence: 99%
“…The adsorption of chitosan from a sodium acetate buffer was tentatively fitted with the Langmuir model [18] or the Freundlich one [19] but none of them applied, suggesting that many different kinds of interactions were involved. Interestingly, the isotherms obtained in ammonium acetate could be fitted by the Freundlich model which writes:…”
Section: Effect Of External Parameters On the Adsorption Of Chitosanmentioning
confidence: 99%
“…The plots of log G versus log C for each isotherm obtained in an ammonium acetate buffer reported in Figure 4 are characterized by a break in the initial slope corresponding to two different adsorption regimes. [19] The first one, at low chitosan concentration, ended at a critical value, C c , for which the second regime took place. These two regimes suggest a difference in conformation of the adsorbed polymer at the surface of the particles.…”
Section: Effect Of External Parameters On the Adsorption Of Chitosanmentioning
confidence: 99%
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