Molecular-weight distribution and structural transformation in water-soluble complexes of poly(acrylic acid) and bovine serum albumin

Topuzogullari M., CIMEN N. S., MUSTAFAEVA Z., MUSTAFAEV M.

EUROPEAN POLYMER JOURNAL, vol.43, no.7, pp.2935-2946, 2007 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 43 Issue: 7
  • Publication Date: 2007
  • Doi Number: 10.1016/j.eurpolymj.2007.04.025
  • Journal Name: EUROPEAN POLYMER JOURNAL
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.2935-2946
  • Keywords: polyelectrolyte, protein, polycomplex, size-exclusion chromatography with quadruple detection, SIZE-EXCLUSION CHROMATOGRAPHY, PERFORMANCE LIQUID-CHROMATOGRAPHY, LIGHT-SCATTERING, ANTIGEN-SPECIFICITY, POLYACRYLIC-ACID, HYBRIDOMA CLONES, IMMUNE-RESPONSE, PROTEIN COMPLEX, SYNTHETIC POLYELECTROLYTES, AFFINITY
  • Yıldız Technical University Affiliated: Yes

Abstract

Interaction of polyacrylic acid (PAA) with bovine serum albumin (BSA) at different pH values and in a wide range of mixing molar ratios, gamma = n(BSA)/n(PAA), of components was investigated by size-exclusion high performance liquid chromatography with on-line refractive index, UV, light scattering and viscometer detectors. The results revealed the formation of stable water-soluble polymer-protein complexes at pH 5.0. For the soluble complexes thus formed, the number of the bound BSA molecules with one PAA molecule was expressed by a Langmuir-type equation as a function of the amount of excess BSA existing free in the solution. At saturation, one BSA molecule is bound to about 48 acrylic acid residues.