Plasma protein adsorption to anion substituted poly(vinyl alcohol) membranes | Zendy

Kyu Eun Ryu | Zendy; Hyang Shuk Rhim | Zendy; Chong Won Park | Zendy; Heung Jae Chun | Zendy; Seung Hwa Hong | Zendy; Jae Jin Kim | Zendy; Young Moo Lee | Zendy

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Plasma protein adsorption to anion substituted poly(vinyl alcohol) membranes

Author(s) -

Kyu Eun Ryu,

Hyang Shuk Rhim,

Chong Won Park,

Heung Jae Chun,

Seung Hwa Hong,

Jae Jin Kim,

Young Moo Lee

Publication year - 2003

Publication title -

macromolecular research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.491

H-Index - 49

eISSN - 2092-7673

pISSN - 1598-5032

DOI - 10.1007/bf03218975

Subject(s) - vinyl alcohol , adsorption , membrane , protein adsorption , nanochemistry , blood proteins , materials science , albumin , polymer chemistry , chromatography , nuclear chemistry , chemistry , organic chemistry , biochemistry , polymer

Anion-substituted poly(vinyl alcohol) (PVA) membranes, carboxymethylated PVA (C-PVA), and sulfonated PVA (S-PVA) were prepared and the effects of these substitutions on the plasma protein adsorption were studied by one- and two-dimensional gel electrophoresis and immunoblotting. When Cuprophane was used as a negative con- trol, the amount of total proteins bound to samples decreased in the order Cuprophane PVA C-PVA S-PVA, which we attribute to the effects of the surface characteristics of the samples, such as their surface tensions and elec- trostatic properties, on the adsorption of proteins to the surfaces of the materials. The results revealed that albumin was the most abundant protein in all the samples. The proportion of adsorbed fibrinogen to S-PVA exceeded those of PVA and C-PVA, whereas S-PVA exhibited the lowest IgG adsorption affinity among the samples we studied.

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