PORE-SIZE CONTROLLED AND POLY(?-LYSINE)-IMMOBILIZED CELLULOSE SPHERICAL PARTICLES FOR REMOVAL OF LIPOPOLYSACCHARIDES
| Autor: | Masami Todokoro, Masashi Kunitake, Masayo Sakata, Kunio Ohkuma, Satoshi Matama, Chuichi Hirayama |
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| Rok vydání: | 2002 |
| Předmět: |
Chromatography
biology Chemistry Clinical Biochemistry Pharmaceutical Science Biochemistry Analytical Chemistry Gel permeation chromatography Matrix (chemical analysis) chemistry.chemical_compound Adsorption Covalent bond Ionic strength Selective adsorption biology.protein Bovine serum albumin Cellulose |
| Zdroj: | Journal of Liquid Chromatography & Related Technologies. 25:601-614 |
| ISSN: | 1520-572X 1082-6076 |
| DOI: | 10.1081/jlc-120003349 |
| Popis: | Poly(ϵ-lysine) was covalently immobilized onto cellulose spherical particles and used for selective adsorption of pyrogenic lipopolysaccharides (LPS) from protein solutions. The resulting poly(ϵ-lysine)-immobilized cellulose particles (PL-cellulose), which had diameters of 44 to 105 μm and matrix's pore-sizes of 2 × 103, 1 × 104, and >2 × 106 as molecular mass exclusions (Mlim), were used as adsorbents. The adsorption of LPS and protein to the adsorbent were determined using a batchwise method. The larger the pore size (Mlim) of the adsorbent, the larger is the LPS-adsorbing activity of the adsorbent. The apparent dissociation constant between the LPS (E. coli O111:B4) and the adsorbent decreased from 3.8 × 10−10 to 1.1 × 10−11 M with an increase in the Mlim from 2 × 103 to >2 × 106 at an ionic strength of μ = 0.05 and a pH of 7.0. On the other hand, the adsorbing activity of bovine serum albumin also increased with the increasing Mlim of the adsorbent, but sharply decreased with increasing ionic strength... |
| Databáze: | OpenAIRE |
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