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Bound components were eluted [100 mM glycine/HCl (pH 2.7)], collected in 1-ml neutralized fractions [100 mM Tris/HCl (pH 9)] and analysed by SDS/PAGE and silver staining.
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Components were eluted with an isocratic system of 5 mM H2SO4 in H2O.
In these separations, a biomolecule such as an enzyme binds to a substrate attached to the solid phase while other components are eluted.
After extensive washing, bound materials were eluted with Laemmli buffer and analysed by immunoblotting.
Spirochetes incubated in EDTA-treated NHS were washed extensively and bound proteins were eluted.
The column was washed extensively and bound proteins were eluted by reduction of the biotin conjugate.
After extensive washing with CB300, bound complexes were eluted with FLAG-peptide and separated by SDS-PAGE.
Unbound proteins were removed and bound proteins were eluted competitively with a concentrated RMS-P3/RR peptide solution.
After 10 cycles of washing with 1x TBS, bound phages were eluted using 0.2 M glycine, pH 2.2.
Subsequently, bound phosphopeptides were eluted under acidic conditions.
After incubation with the sera, the beads were washed, and bound antibodies were eluted.
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