Biochimica et Biophysica Acta (BBA) - Protein Structure
SS-interchanged and oxidized isomers of bovine serum albumin separated by isoelectric focusing
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Quantitative pH assessment of small-volume samples using a universal pH indicator
2014, Analytical BiochemistryDetermination of the ratio between mercaptalbumin and nonmercaptalbumin by HPLC with fluorescence probe specifically binding to albumin
2014, Journal of Pharmaceutical and Biomedical AnalysisCitation Excerpt :Human serum albumin (HSA) is composed of mercaptalbumin (HMA) with a free thiol group on Cys-34, nonmercaptalbumin 1 (HNA1) with Cys-34 bound to cystein or glutathione by a disulfide bond, and nonmercaptalbumin 2 (very small amount) with Cys-34 oxidized to sulfenic, sulfinic or sulfonic [1–4].
HPLC separation of human serum albumin isoforms based on their isoelectric points
2014, Journal of Chromatography B: Analytical Technologies in the Biomedical and Life SciencesCitation Excerpt :Since MS analysis unequivocally confirmed the nature of HSA–SH, we conclude that the real pI of HSA–SH should be higher than 4.9. From the methodological point of view, the most relevant antecedent of this method applied to serum albumins is the report on column isoelectrofocusing of bovine serum albumin (BSA) in water and urea 6 M by Wallevik [45]. This previous report and 2-dimensional polyacrylamide gel electrophoresis practices suggest that the EPGC procedure could be performed in denaturing conditions too.
Effect of ageing of human serum albumin in vitro on surface hydrophobicity and binding sites of metronidazole
2011, Journal of Molecular StructureCitation Excerpt :The N–A transition causes a decrease of the helical content from 55% to 48% [1]. The aged albumin has a higher isoionic point than the albumin with one free SH-group at Cys-34 [2]. The pH affects the binding of many ligands to albumin.
Thiol dependent isomerization of bovine albumin
2009, International Journal of Biological MacromoleculesIntravenous iron administration induces oxidation of serum albumin in hemodialysis patients
2004, Kidney International
Part of this paper was presented at the 9th meeting of the Federation of European Biochemical Societies, August 1974, Budapest, Hungary.