Abstract
Sodium azide is used as an anti-fungal agent in protein samples in the health related scientific community. Due to its toxic nature, monitoring of the azide level in proteins utsed in scientific research is necessary. Ion-exchange chromatography has been used to quantitate azide levels in protein samples. Anion-exchange methodology is described which allows for the separation of azide from various common anions found in analytical grade protein matrices. The analytical system described utilizes a polymer [Poly(styrene—dinivylbenzene)] stationary phase which has been surface sulfonated followed by the binding of the aminated latex bead active ion-exchange sites (Dionex, AS4A column). Sodium tetraborate is used as the weak anion-exchange mobile phase. A vendor ion-exchage column comparison is made along with eluent composition and selection studies. Method validation data are presented including: calibration plots for external standardization, limit of detection and method recovery. Various types of proteins are assayed using the described method.
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