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Isolation and Characterization of Immunoglobulin in Yolk (IgY) Specific against Hen Egg White Lysozyme by Immunoaffinity Chromatography.

Posted by on in 2002
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Chen CC, Tu YY, Chen TL, Chang HM
J Agric Food Chem 2002 Sep 50:5424-8

Abstract
Six hens were intramuscularly (im) immunized once a week for 3 weeks using chicken egg white lysozyme (LS) as antigen. Antibody (immunoglobulin in yolk, IgY) ELISA values of 10(3)-fold diluted yolk were almost as high as 1.879 in the sixth week and maintained a value of 0.756 in the eighth week after the initial immunization treatment. The purification efficiency (specific activity of purified IgY against LS/specific activity of antibody in yolk against LS) of IgY specific against LS isolated by laboratory-prepared LS-bound (IgY-) Sepharose 4 Fast Flow immunoaffinity column was approximately 3380. By applying various amounts (0-22 mg) of the thusly obtained IgY specific against LS to the immunoaffinity column, the binding capacity (q(m)) and dissociation constant (K(d), M(-)(1)) of such immunoaffinity gel for IgY against LS were found to be 0.68 mg of IgY/mL of wet gel (0.54 mg of IgY/mg of LS) and 7.13 x 10(-)(6) M, respectively, as determined by Langmuir-type adsorption isotherms.

Author Address
Department of Food Health, Chia-Nan University of Pharmacy and Science, Tainan 717, Taiwan, and Graduate Institute of Food Science and Technology, National Taiwan University, Taipei 106-17, Taiwan.

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