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

Ostatná, Veronika; Uslu, Bengi; Dogan, Burgu; Özkan, Síbel A.; Paleček, Emil

doi:10.1016/j.jelechem.2006.03.037

Cited by 74 publications

(93 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Obviously, denatured proteins approach randomly coiled conformation [16] but similarly to natively unfolded proteins they may contain some distribution of structures involving short range and long range interactions [17]. Our results [10,11,18] show great potentialities of peak H in discrimination between different proteins and their redox and oxidized forms. More work will be, however, necessary to exploit all potentialities of this peak.…”

Section: Resultsmentioning

confidence: 74%

“…Previously we showed large differences in the peak H heights of native and denatured BSA and other proteins [10,11]. Here we wish to study the effect of CPS parameters on the BSA peak and compare CPS with voltammetric measurements.…”

Section: Resultsmentioning

confidence: 99%

“…Using BCR recently we observed differences between the DC polarograms (with dropping mercury electrode (DME)) of native and denatured bovine serum albumin (BSA), while DC voltammetry (with hanging mercury drop electrode (HMDE)) of the same samples did not discriminate native from denatured BSA [10]. In the same time we showed that native and denatured BSA and other proteins can be discriminated by constant current chronopotentiometric stripping analysis (CPSA) at HMDE in absence of cobalt ions [10].…”

Section: Introductionmentioning

confidence: 99%

“…In the same time we showed that native and denatured BSA and other proteins can be discriminated by constant current chronopotentiometric stripping analysis (CPSA) at HMDE in absence of cobalt ions [10]. BSAwas denatured either by urea or by guanidium chloride (GdmCl) and the measurements of both native and denatured proteins were performed at nondenaturing concentrations of these agents (usually bellow 0.1 M).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Constant Current Chronopotentiometry and Voltammetry of Native and Denatured Serum Albumin at Mercury and Carbon Electrodes

et al. 2008

Self Cite

View full text Add to dashboard Cite

Constant current chronopotentiometric peak H at mercury electrodes was recently shown as a sensitive tool for global and local changes in protein conformation [1]. Large differences between the heights of peak H of native (hBSA nat ) and denatured BSA (hBSA den ) were observed. The ratio hBSA den /hBSA nat increased with more negative stripping current suggesting that the rate of potential change is important for discrimination between native and denatured BSA. Voltammetric peaks of BSA were less well developed and BSA den /BSA nat was much smaller. It was not possible to discriminate BSA den and BSA nat using carbon electrodes.

show abstract

Section: Resultsmentioning

confidence: 74%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Constant Current Chronopotentiometry and Voltammetry of Native and Denatured Serum Albumin at Mercury and Carbon Electrodes

et al. 2008

Self Cite

View full text Add to dashboard Cite

show abstract

“…It is widely applied to determination of proteins for many years since the first papers on polarography of proteins were reported at the beginning of the 1930's. 7,8 For proteins containing cysteine/cystine, their electrochemical signals can be used for quantitative determination based on the formation of Hg-S bonds, 9 the reduction of disulfide groups, 10 and the catalytic evolution of hydrogen 11,12 on mercury electrodes. However, those proteins containing tyrosine and/or tryptophan residues can be oxidized at a carbon electrode.…”

Section: Introductionmentioning

confidence: 99%

Square Wave Voltammetric Label‐free Determination of the Natural Protein Material Silk Fibroin

Song

2008

Chin. J. Chem.

View full text Add to dashboard Cite

The electrochemical behavior of silk fibroin (SF) was investigated by cyclic voltammetry and square wave voltammetry in 0.01 mol/L HCl for the first time. Within the potential scan range of 0.0 to1.2 V (vs. SCE), two oxidative peaks at 0.91 V (P a,1 ) and 0.43 V (P a,2 ) as well as one reductive peak at 0.24 V (P c ) were observed on cyclic voltammogram at scan rate of 0.2 V/s. The peak current of the peak P a,1 was linear with SF concentration in the range of 5.8×10 -8 to 1.1×10 -6 mol/L, with the limit of detection 3.0×10 -8 mol/L (S/N＝3). The proposed method was of high selectivity without the interferences from the coexisting substances such as another natural protein material sericin and other small molecular substances. It was applied to the determination of SF in raw silk liquid samples without any pre-separation and pre-purification.

show abstract

Electrochemical Detection of Proteins

Bartošík

Doneux

Pechan

et al. 2009

Encyclopedia of Analytical Chemistry

View full text Add to dashboard Cite

The advantages of electrochemical methods, such as low cost, rapidity, and sensitivity, make these methods very promising in the booming fields of proteomics and biomedicine. Electroanalysis of proteins relies on redox properties of nonprotein centers within conjugated proteins, application of various labels attached to the protein molecule, or label‐free detection of nonconjugated proteins based on their intrinsic electroactivity. Until recently, electrochemistry of proteins was mainly focused on a relatively small group of conjugated proteins, yielding reversible electrochemistry. This article discusses the new methods that were developed to detect and analyze practically all proteins. Different strategies for electrochemical detection of proteins are presented. Electrode modification by biomolecular receptors (antibodies, aptamers) and their potential use for detection of specific proteins, e.g. disease markers, can be utilized in the development of various sensors. Label‐free electrochemical study of nonconjugated proteins, involving impedance measurements at various electrodes, faradaic signals of tyrosine and tryptophan residues at carbon electrodes and cysteine residues, and electrocatalytic signals at mercury and solid amalgam electrodes have been used. Among them, well‐developed chronopotentiometric peak (peak H) due to catalytic hydrogen evolution shows remarkable sensitivity to local and global changes in protein structure. Recent developments in protein electrochemistry open the way for application of electrochemical analysis in proteomics and biomedicine.

show abstract

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

Cited by 74 publications

References 20 publications

Constant Current Chronopotentiometry and Voltammetry of Native and Denatured Serum Albumin at Mercury and Carbon Electrodes

Constant Current Chronopotentiometry and Voltammetry of Native and Denatured Serum Albumin at Mercury and Carbon Electrodes

Square Wave Voltammetric Label‐free Determination of the Natural Protein Material Silk Fibroin

Electrochemical Detection of Proteins

Contact Info

Product

Resources

About