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, cilt.43, sa.7, ss.2935-2946, 2007 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 43 Sayı: 7
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1016/j.eurpolymj.2007.04.025
  • Dergi Adı: EUROPEAN POLYMER JOURNAL
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.2935-2946
  • Anahtar Kelimeler: 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 Teknik Üniversitesi Adresli: Evet

Özet

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.