Native and denatured bovine serum albumin. D.c. polarography, stripping voltammetry and constant current chronopotentiometry

Ostatna V., Uslu B., Dogan B., ÖZKAN S. A., Palecek E.

JOURNAL OF ELECTROANALYTICAL CHEMISTRY, cilt.593, sa.1-2, ss.172-178, 2006 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 593 Sayı: 1-2
  • Basım Tarihi: 2006
  • Doi Numarası: 10.1016/j.jelechem.2006.03.037
  • Dergi Adı: JOURNAL OF ELECTROANALYTICAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.172-178
  • Anahtar Kelimeler: protein electrochemistry, native and denatured proteins, mercury electrodes, adsorptive stripping, constant current chronopotentiometry, bovine serum albumin, TOBACCO-MOSAIC-VIRUS, HYDROGEN EVOLUTION, MERCURY-ELECTRODES, PROTEINS, METALLOTHIONEIN, REDUCTION, PEPTIDES, BEHAVIOR, IONS, DNA
  • Ankara Üniversitesi Adresli: Evet

Özet

Native and denatured states of bovine serum albumin (BSA) were studied by d.c. polarographic and voltammetric Brdicka catalytic responses (BCR) in cobalt-containing solution and by constant current chronopotentiometric stripping analysis (CPSA) in borate buffer, pH 9.3. We found that 90 nM denatured BSA produced catalytic peak H (around -1.8 V vs. Ag/AgCl/3 M KCl). This peak was about 50-fold higher than the native protein under the same conditions. Qualitatively similar results were obtained also with other proteins in native and denatured states, such as human serum albumin, gamma-globulin, myoglobin and a-crystallin. 2 nM denatured BSA produced a well-developed CPS peak (at accumulation time 5 min) while native BSA yielded almost no signal under the same conditions. (c) 2006 Elsevier B.V. All rights reserved.