A thermodynamic study of the binding of human serum albumin onto N,N '-diethylaminoethyl dextran microbeads

Can H., Guner A.

JOURNAL OF APPLIED POLYMER SCIENCE, cilt.101, sa.6, ss.3942-3947, 2006 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 101 Sayı: 6
  • Basım Tarihi: 2006
  • Doi Numarası: 10.1002/app.22894
  • Dergi Adı: JOURNAL OF APPLIED POLYMER SCIENCE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.3942-3947
  • Hacettepe Üniversitesi Adresli: Evet

Özet

Adsorption of proteins on solid surfaces is widely studied because of its importance in various biotechnological, medical, and technical applications, e.g., biosensors, cardiovascular implants, and chromatography. Adsorption thermodynamics has been studied on the microbeads of N,N'-diethylaminoethyl (DEAE) Dextran anion exchanger for the human serum albumin (HSA) at 25, 30, 35, 40, and 45 degrees C. As a result, some thermodynamic parameters like Freundlich constants, thermodynamic equilibrium constant (K-D), standard free energy changes (Delta G(assoc)), standard entropy changes (Delta S-assoc), and standard enthalpy change have been evaluated. Using the linear Van't Hoff plot, Delta S-assoc value of the system for the interaction of bovine serum albumin (BSA)-adsorbed crosslinked DEAE dextran microbeads was determined as 20.650 kJ/mol. (c) 2006 Wiley Periodicals, Inc.