作者: Tova Kukulansky , Nurit Hollander , Shirley Abramovitch
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摘要: Thy-1 protein, a member of the Ig superfamily, is bound to cell membrane by glycosylphosphatidylinositol (GPI) anchor. We demonstrate that following anchor cleavage phospholipase C, reactivity solubilized with several mAbs lost, and its polyclonal anti-Thy-1 Abs markedly decreased. Hence, cannot be detected range mAbs. In contrast, enzymatic biotinylated yields an intact protein can streptavidin. These results exclude possible proteolytic degradation suggest marked decrease in immunoreactivity delipidation due conformational changes protein. further addition C preformed Ab-Ag complexes causes dissociation removal from complex, indicating induces change sufficient dissociate Ab. The possibility should therefore considered GPI affects conformation which it linked.