کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
10533069 961845 2005 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Characterization of polyanion-protein complexes by frontal analysis continuous capillary electrophoresis and small angle neutron scattering: Effect of polyanion flexibility
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Characterization of polyanion-protein complexes by frontal analysis continuous capillary electrophoresis and small angle neutron scattering: Effect of polyanion flexibility
چکیده انگلیسی
The binding constant (Kobs) for the β-lactoglobulin-poly(vinylsulfate) (BLG-PVS) complex was measured by frontal analysis continuous capillary electrophoresis at pH values above the isoelectric point of BLG, and the persistence length (Lp) of PVS was measured by small angle neutron scattering, to examine the effect of polyelectrolyte chain stiffness on its binding efficiency to proteins. The values of Kobs and Lp were compared with those of BLG-PSS and BLG-PAMPS (poly(2-acrylamido-2-methylpropanesulfonate)) reported previously. The relationship between Kobs and Lp was reciprocal, indicating that protein binding is enhanced by the flexibility of the polyanion, at least in the case where the net protein charge is negative. In addition, at a fixed pH, the polymer systems displayed a similar ionic strength dependence of Kobs. This similarity was consistent with the proposal that the binding properties of PVS and PAMPS polyanions are governed purely by electrostatic interactions and are independent of their molecular structure.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Analytical Biochemistry - Volume 342, Issue 2, 15 July 2005, Pages 229-236
نویسندگان
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