203Hg labelled PHMB as reagent for the determination of –SH groups in native and denatured proteins by hydrophobic interaction chromatography

Autor: Giorgio Raspi, G. Tesi, Maria Spinetti, Emilia Bramanti
Rok vydání: 1999
Předmět:
Zdroj: The Analyst. 124:511-515
ISSN: 1364-5528
0003-2654
DOI: 10.1039/a809381d
Popis: 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 203Hg-labelled p-hydroxymercuribenzoate as reagent and known concentrations of proteins. The results were compared with FI-CV-ETAAS measurements and literature data.
Databáze: OpenAIRE