Improving the reliability of human serum albumin-thiol group determination

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

doi:10.1016/j.ab.2013.03.033

Cited by 17 publications

(10 citation statements)

References 33 publications

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“…The supernatant was collected and stored at 80°C. A differential ammonium sulphate precipitation two-step protocol described by Mandia's team (66) and modified in our lab (67) was used to extract HSA from the plasma. The first step consisted of adding 54% of ammonium sulphate (AS) to a plasma sample using a saturated 100% AS solution (540 g/L; pH adjusted to 7.4 with NH 4 OH).…”

Section: Methodsmentioning

confidence: 99%

Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

Soudahome

Catan

Giraud

et al. 2018

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

Soudahome

Catan

Giraud

et al. 2018

Journal of Biological Chemistry

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“…31 The free sulydryl group content is a parameter of the redox state of the protein. Anti-oxidative activity of HSA is one of the important functional property which resides in one free cysteine-derived redox-reactive thiol (-SH) group (Cys34), exists in both reduced and oxidized forms.…”

Section: Thiol Group Estimationmentioning

confidence: 99%

Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

2015

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Early glycation involves attachment of glucose on 3-NH 2 of lysine residues. Human serum albumin (HSA), a lysine rich protein, is highly prone to non-enzymatic glycation. In this study, the effect of different concentrations of glucose on HSA through early glycation was assessed by various physicochemicaltechniques. An early glycation product Amadori HSA was estimated by colorimetric method, nitro blue tetrazolium (NBT) and thiobarbituric acid assay (TBA). The conformational changes were confirmed by UV-visible spectroscopy, tryptophan fluorescence quenching, circular dichroism (CD), and sodium dodecyl sulphate poly acrylamide gel electrophoresis (SDS-PAGE). Biochemical alterations in Amadori-HSA were analyzed by NaBH 4 reduction, increased carbonyl content and decrease in free lysine, arginine and sulfhydryl groups. Most studies have reported the structural changes in protein due to AGEs or Amadori protein at a particular glucose concentration; to the best of our knowledge, no reports have been published comparing the physicochemical changes in HSA due to early glycation within a range of glucose concentrations. In the present study, the investigations confirmed the structural and biochemical alterations in Amadori-HSA which is directly proportional to glucose concentration. This might interfere with the normal function of HSA and can contribute to the progression of diabetes and its associated complications. Amadori modified HSA might be used as a biomarker for early detection of diabetes and be beneficial in preventing the diabetic complications at early stages of diabetes. In this context, this study provides additional information about biochemical and biophysical changes occurring in Amadori-HSA within the glucose range upon early glycation.

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“…OS is reported to be involved in many diseases and syndromes. [5][6][7] Nonetheless, until recently in trials aimed at evaluating OS, usually quite complicated methods like high-sensitivity fluorometric high-performance liquid chromatography, 8 capillary electrophoresis with laserinduced fluorescence detection 9 and enzymatic recycling, 10 and substances such as 5,5 ′ -dithiobis-(2-nitrobenzoic acid) (DTNB) 11 and dithiodipyridine (4-DPS) 12 were used.…”

Section: Introductionmentioning

confidence: 99%

Thiol/disulphide homeostasis in pregnant women with Familial Mediterranean fever

et al. 2016

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Improving the reliability of human serum albumin-thiol group determination

Cited by 17 publications

References 33 publications

Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

Impact of in vitro non-enzymatic glycation on biophysical and biochemical regimes of human serum albumin: relevance in diabetes associated complications

Thiol/disulphide homeostasis in pregnant women with Familial Mediterranean fever

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