Adsorption of human IgG on to poly(N-isopropylacrylamide)-based polymer particles
| Autor: | José M. G. Martinho, Andrea Santos, Claudia S. O. Silva, M. Ângela Taipa, Joaquim M. S. Cabral, Ricardo P. Baptista |
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| Rok vydání: | 2006 |
| Předmět: |
Steric effects
Time Factors Polymers Acrylic Resins Bioengineering Applied Microbiology and Biotechnology Human Immunoglobulin G chemistry.chemical_compound Adsorption Polymer chemistry Humans Methyl methacrylate chemistry.chemical_classification Acrylamides Temperature General Medicine Polymer Hydrogen-Ion Concentration Poly(methyl methacrylate) Polymer particle chemistry Immunoglobulin G visual_art visual_art.visual_art_medium Poly(N-isopropylacrylamide) Nanoparticles Biotechnology Nuclear chemistry |
| Zdroj: | Biotechnology Letters. 28:2019-2025 |
| ISSN: | 1573-6776 0141-5492 |
| DOI: | 10.1007/s10529-006-9188-2 |
| Popis: | Thermosensitive poly(N-isopropylacrylamide)-based polymer particles were synthesised, and screened for the adsorption of human immunoglobulin G (hIgG). At pH 9 the adsorption on microgel particles was strongly affected by temperature, approximately 40 mg hIgG/g support (90% of initial hIgG) being adsorbed at 40 degrees C but only 10% of initial hIgG at 25 degrees C. At pH 5 the maximum adsorbed amount (20 mg hIgG/g support) was similar for both temperatures. The adsorption of hIgG on to charged poly(methyl methacrylate)/poly(N-isopropylacrylamide) core-shell latexes was negligible (5-10 mg hIgG/g support) at the same temperature and pH conditions. The lower adsorption of hIgG onto the core-shell particles is explained by steric interactions due to the small size of the shell. |
| Databáze: | OpenAIRE |
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