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Maackia fauriei 유래 렉틴에 대한 IgY 항체의 생성 및 분리
정영윤(Young Yun Chung),정의차(Eui Cha Jung),이현정(Hyun Jung Lee),김하형(HaHyung Kim) 대한약학회 2005 약학회지 Vol.49 No.1
Immunoglobulin Y (IgY) obtained from chicken as the immunization host brings several advantages to antibody production, such as improved yield, lower cost, longer stability, and higher specificity than mammalian immunoglobulin. In the present study, we attempted to produce IgY against a sialic acid-binding lectin, Maackia fauriei agglutinin(MFA), from egg yolk of white Leghorn hens. For the isolation of IgY from egg yolk, we applied a water dilution method. The weekly yield of IgY was determined by enzyme-linked immunosorbent assay, with a final yield of anti-MFA IgY from total IgY of approximately 1%. The yielded IgY were used to prepare IgY-affinity column conjugated with CNBr-activated Sepharose 4B, which resulted in the lectin being successfully purified in a single step from Maackia fauriei. This purified lectin exhibited the same hemagglutination activity as lectin purified using conventional purification methods.