摘要

It is difficult to isolate the specific egg yolk antibody (IgY) from large amounts of accompanied nonspecific ones with the usually exploited techniques. In this article, using immunogen bacteria as receptors, an affinity chromatography was developed for separation of specific IgY. Listeria monocytogens cells were amino activated with divinyl sulfone to increase the binding efficiency between cells and Sepharose 4B. After the modification, the separation efficiency of corresponding columns was estimated to be four to six times those of untreated cells. The results allowed us to suggest a hopeful application of the established method for production of high-purity antibacterial-specific IgY.