The influence of fatty acids on determination of human serum albumin thiol group

Jovanović, Vesna; Pavićević, Ivan D.; Takić, Marija; Penezić-Romanjuk, Ana Z.; Aćimović, Jelena M.; Mandić, Ljuba M.

doi:10.1016/j.ab.2013.11.030

Cited by 16 publications

(21 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Commercial HSA contains approximately 0.4 mol-SH group/ mol HSA, so commercial defatted HSA was reduced with dithiothreitol (DTT) [14]. Prior to the reduction the content of HSA-SH group was determined.…”

Section: Preparation Of Reduced Hsa (Mercaptoalbumin)mentioning

confidence: 99%

“…Free HSA-SH content was determined spectrophotometrically according to a modified Ellman's method [14,33]. 5,5 0 -dithiobis (2-nitrobenzoic acid) (DTNB) reagent (100 lL of 2 mmol/L solution) was mixed with equal volumes of sample and 1 mol/L Tris buffer (pH 8.0) and brought up to 1000 lL with distilled water.…”

Section: Quantification Of Hsa and Hsa-thiol Group Contentmentioning

confidence: 99%

“…However, FAs binding change the reactivity of HSA-SH and modify its reaction kinetics with hydrogen peroxide and peroxynitrite [14][15][16], suggesting the possibility of modulation of HSA antioxidative capacity when some FAs were supplemented in the diet. On the other hand, in pathological conditions with hyperlipidemia and carbonyl stress, the increased reactivity of the thiol group (as consequence of free FAs binding to HSA), could lead to the increase of its potential to scavenge reactive carbonyl species.…”

Section: Introductionmentioning

confidence: 99%

“…These latter compounds exhibit significantly enhanced reactivity for sites such as arginine and lysine residues on proteins, resulting in the creation of advanced glycation endproducts (AGEs) [20,23]. All mentioned reactions lead to decrease in the content of Lys, Arg and Cys residues on the HSA surface in diabetes [14,[24][25][26].…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal

Pavićević

Jovanović

Takić

et al. 2014

Chemico-Biological Interactions

Self Cite

View full text Add to dashboard Cite

Section: Preparation Of Reduced Hsa (Mercaptoalbumin)mentioning

confidence: 99%

Section: Quantification Of Hsa and Hsa-thiol Group Contentmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal

Pavićević

Jovanović

Takić

et al. 2014

Chemico-Biological Interactions

Self Cite

View full text Add to dashboard Cite

“…22 Binding of FA is associated with significant structural changes in the HSA molecule, 23 which can cause the Cys34 residue to be more or less exposed to the surrounding environment, leading to differential reactivity and susceptibility to oxidative stress. [19][20][21][24][25][26][27] These findings lead to the question: Does the binding of EL and ED to HSA (for which the antioxidant effect is proven) influence HSA-SH reactivity and therefore its antioxidant potential? Although numerous studies on the interactions between polyphenols and HSA have been performed, the changes in HSA-SH reactivity that can occur upon polyphenol binding (which may be relevant to antioxidant properties) have not been considered yet.…”

Section: Introductionmentioning

confidence: 99%

Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity

et al. 2016

Self Cite

View full text Add to dashboard Cite

The interaction of polyphenolic molecules with human serum albumin (HSA) could lead to changes in the reactivity of the HSA Cys34 thiol group (HSA-SH). The influences of enterolactone (EL) and enterodiol (ED) binding on HSA-SH reactivity in fatty acid (FA)-free HSA, and in HSA with bound stearic acid (S) in S/HSA molar ratios of 1 : 1 and 4 : 1, were investigated by the determination of the pseudo first order rate constants (k') for the thiol reaction with 5,5'-dithiobis-(2-nitrobenzoic acid). The binding affinities and binding sites of EL and ED were also determined, using fluorescence measurements of the intrinsic fluorescence ). When the S/HSA ratio was increased, the binding affinities and number of binding sites for EL and ED were decreased. At the same time, a high correlation between binding constants and increased Cys34 reactivity was found (r = 0.974). Competitive experiments using diazepam indicated that the binding of ED and of EL was located in the hydrophobic pocket of site II in HSA. Overall, it is evident that stearic acid could modulate the enterolignan effects on HSA-SH reactivity as well as their binding to HSA. This finding could be important for pharmacokinetics and the expression of enterolignan antioxidant effects in vivo after an intake of lignan rich food.

show abstract

Simultaneous optical detection of human serum albumin and transferrin in body fluids

Rasouli

Ghavami

2020

Microchim Acta

View full text Add to dashboard Cite

The influence of fatty acids on determination of human serum albumin thiol group

Cited by 16 publications

References 39 publications

Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal

Fatty acids binding to human serum albumin: Changes of reactivity and glycation level of Cysteine-34 free thiol group with methylglyoxal

Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity

Simultaneous optical detection of human serum albumin and transferrin in body fluids

Contact Info

Product

Resources

About