Linked Life Data

12885522

Source:http://linkedlifedata.com/resource/pubmed/id/12885522

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-7-29
pubmed:abstractText
Weak amphoteric charged membranes were prepared by the graft copolymerization of poly(ethylene glycol) (PEG) derivatives with pendant ionizable groups onto polyethylene (PE) porous membranes. Two types of weak amphoteric charged membranes and two types of weak single charged membranes were prepared. The pH dependence of the protein (fluorescein isothiocyanate-labeled bovine serum albumin, FITC-BSA) adsorption onto the membranes was investigated by fluorescence spectroscopy. The interfacial charge properties of the membranes and protein were also characterized at different pH values by streaming potential and electrophoretic light scattering (ELS) measurements, respectively. The adsorbed amount onto each ionic PEG chain grafted membrane showed a uniform maximum value near the isoelectric point (IEP) of the protein (pH 4.1). On both sides of the IEP (pHs 3.3 and 7.2), the adsorption experiments and zeta (zeta) potential measurements were well correlated: the contribution of electrostatic interaction was dominant for the protein adsorption behavior. In the alkaline condition (pH 10.2), the adsorption experiments contradict the zeta potential measurements. It suggested that the conformational change of protein molecule influenced the adsorption behavior. Finally, these results indicated the potential of controlling the protein-ionic PEG chain interaction on the membrane surfaces by the pH adjustment of the outer solution.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9797
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
82-8
pubmed:dateRevised
2009-11-11
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Interaction of proteins with weak amphoteric charged membrane surfaces: effect of pH.
pubmed:affiliation
Department of Organic and Polymeric Materials, and International Research Center of Macromolecular Science, Tokyo Institute of Technology, 2-12-1 Ookayama, Meguro-ku, Tokyo 152-8552, Japan.
pubmed:publicationType
Journal Article