【摘 要】
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Some unique subclasses of Camelidae antibodies are devoid of the light chain,and the antigen binding site is comprised exclusively of the variable domain of
【出 处】
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2014年全国生物技术与食品质量博士后学术论坛
论文部分内容阅读
Some unique subclasses of Camelidae antibodies are devoid of the light chain,and the antigen binding site is comprised exclusively of the variable domain of the heavy chain(VHH).Therecombinant VHHs have a high potential as alternative reagents for the next generation of immunoassay.In particular,they might be very useful for molecular mimicry.The present study demonstrated an alpaca immunized with the F(ab )2 fragment of anti-aflatoxin B 1 mAb and developedan important anti-idiotypic(anti-Id)responses.Antigen-specific elution method was used for panning private anti-Id VHHs from the constructed alpaca VHH library.The selected VHHs were expressed,renatured,purified,and then identified by a competitive enzyme-linked immunosorbent assay(ELISA).Our findings indicated that the VHH would be an alternative tool for haptens mimicry studies.
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