1997
DOI: 10.1006/jcis.1997.4987
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Interfacial State Change of Cellulose Triacetate Membrane by Adsorption of Polyelectrolyte

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Cited by 14 publications
(10 citation statements)
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“…The pore structure plays an important role in the diffusion of small molecules. In previous papers, the effect of the membrane structure on electrolyte diffusion through this membrane has been discussed (3,4). If the pores are isolated, the polymer matrix presents a high barrier to the diffusion of a penetrant.…”
Section: Introductionmentioning
confidence: 99%
“…The pore structure plays an important role in the diffusion of small molecules. In previous papers, the effect of the membrane structure on electrolyte diffusion through this membrane has been discussed (3,4). If the pores are isolated, the polymer matrix presents a high barrier to the diffusion of a penetrant.…”
Section: Introductionmentioning
confidence: 99%
“…Due to its ability to bind on hydrophobic surfaces (Wertz & Santore, 2002), lysozyme in zein Wlms that are also mainly hydrophobic may be retained by hydrophobic interactions. However, it was reported that in CTA membranes that are also hydrophobic, the lysozyme is absorbed mainly because of the cation-exchange properties of these membranes (Murata & Tonioka, 1997). Further studies are needed to reveal the binding mechanism of lysozyme on zein Wlms and to show the contribution of immobilized lysozyme activity to their antimicrobial eVect.…”
Section: Immobilized Lysozyme Activity Retained In Wlmsmentioning
confidence: 99%
“…The magnitude of r P for PAS-H(10L) corresponds to those in the previous paper within errors (12). On the other hand, the magnitude of r P for albumin and lysozyme is different from those in the previous paper though their flow directions correspond.…”
Section: ϫmentioning
confidence: 51%
“…Protein adsorption by CTA membrane is much affected not only by the conditions of external solution but also by the state of the membrane surface, including the higher order structure. It, however, is so difficult to control the surface structure exactly (12). It is considered that r P discrepancies between those data for protein-adsorbed membrane is resulted in the difference of the adsorption state caused by the different surface state from membrane to membrane.…”
Section: ϫmentioning
confidence: 98%
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