Journal Article


Stéphanie Boullanger
Eric Defrancq
Richard O'Kennedy
Om Prakash Edupuganti
Soujanya Ratna Edupuganti



animals electrophoresis polyacrylamide gel chemistry chromatography affinity surface plasmon resonance metabolism igy enzyme linked immunosorbent assay isolation purification triticum mass spectrometry sensitivity and specificity immunoglobulins chickens instrumentation t 2 toxin reproducibility of results

Use of T-2 toxin-immobilized amine-activated beads as an efficient affinity purification matrix for the isolation of specific IgY. (2012)

Abstract An affinity purification method that isolates T-2 toxin-specific IgY utilizing a T-2-toxin-immobilized column was developed. The T-2 toxin was covalently coupled via a carbonyldiimidazole-activated hydroxyl functional group to amine-activated sepharose beads. The affinity-purified IgY was characterized by gel electrophoresis, fast protein liquid chromatography, enzyme-linked immunosorbant assay, surface plasmon resonance and mass spectrometry. A competitive inhibition ELISA (CI-ELISA) was performed using affinity-purified IgY with a T-2 toxin detection sensitivity of 30 ng/mL, which falls within the maximum permissible limit of 100 ng/mL. The cross reactivity of IgY towards deoxynivalenol, zearalenone, fumonisin B1 and HT-2 was significantly reduced after affinity purification. A surface plasmon resonance (SPR)-based inhibition assay was also applied for quantitative determination of T-2 toxin in spiked wheat samples. The results obtained indicate the feasibility of utilizing this IgY-based assay for the detection of T-2 toxin in food samples.
Collections Ireland -> Dublin City University -> PubMed

Full list of authors on original publication

Stéphanie Boullanger, Eric Defrancq, Richard O'Kennedy, Om Prakash Edupuganti, Soujanya Ratna Edupuganti

Experts in our system

R O'Kennedy
Dublin City University
Total Publications: 197