Aldolase, glyceraldehyde 3-phosphate dehydrogenase and ovalbumin were determined by hydrophobic interaction chromatography, which allows the evaluation of the number of -SH groups per molecule of protein in both the native and denatured form. These proteins were chosen as models to show the generality of use of the procedure for analytical and biochemical applications. The experiments were performed by using Hg-203-labelled p-hydroxymercuribenzoate as reagent and known concentrations of proteins. The results were compared with FI-CV-ETAAS measurements and literature data.
Hg-203 labelled PHMB as reagent for the determination of -SH groups in native and denatured proteins by hydrophobic interaction chromatography
1999
Abstract
Aldolase, glyceraldehyde 3-phosphate dehydrogenase and ovalbumin were determined by hydrophobic interaction chromatography, which allows the evaluation of the number of -SH groups per molecule of protein in both the native and denatured form. These proteins were chosen as models to show the generality of use of the procedure for analytical and biochemical applications. The experiments were performed by using Hg-203-labelled p-hydroxymercuribenzoate as reagent and known concentrations of proteins. The results were compared with FI-CV-ETAAS measurements and literature data.File in questo prodotto:
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