화학공학소재연구정보센터
Journal of Applied Polymer Science, Vol.100, No.2, 1554-1560, 2006
Intermolecular interactions between bovine serum albumin and certain water-soluble polymers at various temperatures
Viscometric behaviors of dextran (Dx), poly(N-vinyl-2-pyrrolidone) (PVP), and poly(ethylene oxide) (PEO) with bovine serum albumin (BSA) in aqueous solutions have been studied at 25, 30, and 35 degrees C. The reduced viscosity and intrinsic viscosity have been experimentally measured for the polymer/water and polymer/BSA/water systems by classical Huggins equation. Measurements of reduced viscosities of the Dx, PVP, and PEO in water have been calculated and all intrinsic viscosities of PEO([eta](PEO)) are larger than that of Dx([eta](Dx)), and PVP([eta](PVP)) in aqueous solutions, at all temperatures. The intrinsic viscosities of PVP, PEO, and Dx were found to be dependent on the concentration of BSA. The presence of BSA (0.05, 0.10, and 0.30 wt %) led to a decrease in the intrinsic viscosities of polymers, at 25, 30, and 35 degrees C. The concentration difference of BSA (A[BSAI) is most effective in decreasing the intrinsic viscosities of Dx at 25 degrees C and PEO at 30 and 35 degrees C. In other words, A[eta] (%) order followed as Dx > PEO > PVP at 25 degrees C and PEO > Dx > PVP at 30 and 35 degrees C. (c) 2006 Wiley Periodicals, Inc.