Interactions of Poly (<I>N</I><SUP>α</SUP>, <I>N</I><SUP>ε</SUP>-terephthaloyl-L-lysine) Membrane for Artificial Red Blood Cells with Serum Proteins
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- SUZUKI Shiro
- Ferris Women's Junior College
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- KONDO Tamotsu
- Faculty of Pharmaceutical Sciences, Science University of Tokyo
Bibliographic Information
- Other Title
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- 人工赤血球ポリ(N?Qα?R,N?Qε?R‐テレフタロイル‐L‐リジン)膜と血清タンパク質の相互作用
- ジンコウ セッケッキュウヨウ ポリ Nアルファ Nイプシロン テレフタロイルー
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Abstract
The interactions between poly (Nα, Nε-terephthaloyl-L-lysine) membrane (PPL membrane), an artificial red cell membrane, and serum proteins were studied at different pH and ionic strengths of the medium. PPL membrane was prepared by an interfacial polycondensation reaction between L-lysine dissolved in the aqueous phase and terephthaloyl dichloride dissolved in the organic phase. The interactions were found to depend strongly on the pH of the medium while the ionic strength had little or no effect. At pH 2.0, the proteins with a high positive net charge were adsorbed on the negatively charged surface of PPL membrane to lower the zeta potential of the microcapsules, thereby causing their aggregation to a great extent. Since the proteins bore only a very low positive net charge at pH 4.0, their electrostatic interactions with the capsules were weak ; the protein adsorption decreased to decline zeta potential lowering and capsule aggregation. Neither protein adsorption nor capsule aggregation was observed at pH 7.0 where both the capsules and the proteins were negatively charged.
Journal
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- KOBUNSHI RONBUNSHU
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KOBUNSHI RONBUNSHU 36 (4), 197-201, 1979
The Society of Polymer Science, Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390001206523647104
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- NII Article ID
- 130004033821
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- NII Book ID
- AN00085011
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- ISSN
- 18815685
- 03862186
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- NDL BIB ID
- 2050663
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed