Mischak H, Neubauer C, Kuechler E, Blaas D
Institut für Biochemie, Wien, Austria.
Virology. 1988 Mar;163(1):19-25. doi: 10.1016/0042-6822(88)90229-2.
The receptor for the minor group of human rhinoviruses was solubilized from HeLa cell membranes with various detergents. Virus binding activity was determined in a filter binding assay using 35S-labeled human rhinovirus 2 (HRV2) as a probe. The receptor protein was enriched on Lens culinaris lectin columns and the active fractions were further purified by gel permeation and anion exchange chromatography. The receptor has an apparent molecular weight of 450 kDa in the presence of detergent. The binding activity is sensitive to trypsin, sulfhydryl modifying agents, but insensitive to neuraminidase. Divalent cations are essential for virus binding.
人类鼻病毒小亚组的受体用各种去污剂从HeLa细胞膜中溶解出来。使用35S标记的人类鼻病毒2（HRV2）作为探针，通过滤膜结合试验测定病毒结合活性。受体蛋白在菜豆凝集素柱上富集，活性组分通过凝胶渗透和阴离子交换色谱进一步纯化。在去污剂存在的情况下，该受体的表观分子量为450 kDa。结合活性对胰蛋白酶、巯基修饰剂敏感，但对神经氨酸酶不敏感。二价阳离子对病毒结合至关重要。
