Purification of immunoglobulins from chicken sera by thiophilic gel chromatography.
Immunoglobulin Y is different from most of the other immunoglobulins because it does not bind protein A or protein G. Thiophilic gel chromatography has been successfully used to purify IgY from chicken egg yolk, but the technology has not previously been used to purify IgY from serum. In this research note, we describe the optimization of T-gel chromatography for purification of IgY from serum. Data are provided on the recovery and purity of IgY obtained using potassium sulfate buffers of different concentrations. Decreasing the strength of potassium sulfate buffer from 0.5 to 0.3 M did not alter the amount of IgY recovered but increased the purity. Using 0.3 M potassium sulphate, we recovered approximately 63.7% of the serum Ig as almost pure IgY.
Constantinoiu
C C
CC
School of Veterinary Science, University of Queensland, Brisbane, Queensland, 4072, Australia. c.constantinoiu@uq.edu.au
Molloy
J B
JB
Jorgensen
W K
WK
Coleman
G T
GT
D000818:Animals; D002645:Chickens / Q000097:blood*; D002850:Chromatography, Gel / Q000662:veterinary*; D007136:Immunoglobulins / Q000097:blood* / Q000302:isolation & purification*; D013431:Sulfates
C016512:IgY; D007136:Immunoglobulins; D013431:Sulfates; C031512:potassium sulfate