Native and denatured bovine serum albumin. D.c. polarography, stripping voltammetry and constant current chronopotentiometry
JOURNAL OF ELECTROANALYTICAL CHEMISTRY, cilt.593, sa.1-2, ss.172-178, 2006 (SCI-Expanded, Scopus)
- 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.