کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9918720 | 1557555 | 2005 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Calorimetric study of bovine serum albumin dilution and adsorption onto polystyrene particles
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کلمات کلیدی
موضوعات مرتبط
علوم پزشکی و سلامت
داروسازی، سم شناسی و علوم دارویی
علوم دارویی
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چکیده انگلیسی
Titration calorimetry was used to investigate the interaction between a model antigen, bovine serum albumin (BSA), and a model particulate carrier, polystyrene (PS). The binding enthalpy was much higher than reported in the literature for a similar system and did not display a sigmoidal binding curve. These experiments may have accessed low coverage surface sites due to the irreversible nature of protein binding and stepwise titration. An important correction is the heat of dilution of the protein solution. Two regimes were observed: at low concentrations of BSA (below ca. 0.3% (w/v)) an exothermic dilution enthalpy of ca. â100Â mJÂ mgâ1 was determined, whereas at higher concentrations of BSA values of ca. â20Â mJÂ mgâ1 were obtained. Solution rheological data also showed a change at 0.3% (w/v) BSA, so we hypothesise that the fraction of the BSA as monomers, dimers and polymers in solution changes at approximately 0.3% (w/v).
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Pharmaceutics - Volume 298, Issue 2, 25 July 2005, Pages 333-338
Journal: International Journal of Pharmaceutics - Volume 298, Issue 2, 25 July 2005, Pages 333-338
نویسندگان
M.J. Pollitt, G. Buckton, S. Brocchini, H.O. Alpar,