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Two millimeter width nitrocellulose strips, containing small squares from the total number of peptides for each of the molecules investigated (GGF, SMDF and NDF), were exposed to IgY antibody diluted 1:100.
After extensive washing, blots were incubated for 1 h with horseradish peroxidase-conjugated rabbit anti-chicken IgY (Pierce Biotechnology, Rockford, IL) diluted 1:2,000 in PBS-Tween 20.
Strips were washed and incubated with HRP-conjugated rabbit anti-chicken IgY (Pierce Biotechnology, Rockford, IL) diluted 1:2,000 in PBS-Tween 20.
Evaluation of purified IgY antibodies by SDS-PAGE analyses showed, in addition to a few weak bands, two protein bands with relative molecular masses of 68 and 25 kDa that correspond to heavy and light chains from Y immunoglobulin, coinciding with the commercial control (Fig.
The immunoglobulin obtained from the eggs-yolk was determined by the absorbance to 280 nm, considering that the IgY extinction coefficient has been calculated to be 1.35 ; therefore, 1.35 UA = 1mg/mL.
The IgY purity was determined by protein polyacrylamide gel electrophoresis (PAGE) at 12% according to Laemmli et al.
In gel diffusion assay using specific IgY against scolopendra venom
To demonstrate the specific IgY immunoglobulin activity, an Ouchterlony double gel diffusion test was used .
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