作者: Harald Mischak , Christoph Neubauer , Ernst Kuechler , Dieter Blaas
DOI: 10.1016/0042-6822(88)90229-2
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摘要: The receptor for the minor group of human rhinoviruses was solubilized from HeLa cell membranes with various detergents. Virus binding activity determined in a filter assay using 35S-labeled rhinovirus 2 (HRV2) as probe. protein enriched on Lens culinaris lectin columns and active fractions were further purified by gel permeation anion exchange chromatography. has an apparent molecular weight 450 kDa presence detergent. is sensitive to trypsin, sulfhydryl modifying agents, but insensitive neuraminidase. Divalent cations are essential virus binding.