Li J K, Fox C F
J Supramol Struct. 1975;3(1):51-60. doi: 10.1002/jss.400030106.
Lactoperoxidase-catalyzed iodination selectively labels the two glycoproteins (VP1 and VP2) of Newcastle disease virus. The low-molecular-weight, nonglycosylated major viral protein, VP6, was not iodinated in the intact virus but was iodinated in disrupted virions, suggesting a localization on the inner, rather than the outer, envelope surface. Studies on the distribution of virion proteins labeled with 125-I and 3-H-isoleucine between detergent-soluble and detergent-insoluble fractions show that the virion proteins VP4, VP5, and VP6 are solubilized to a much lesser extent than are VP1 and VP2.
乳过氧化物酶催化的碘化反应可选择性地标记新城疫病毒的两种糖蛋白(VP1和VP2)。低分子量、非糖基化的主要病毒蛋白VP6,在完整病毒中未被碘化,但在破碎的病毒粒子中被碘化,这表明其定位于内膜而非外膜表面。对用¹²⁵-I和³-H-异亮氨酸标记的病毒粒子蛋白在去污剂可溶和去污剂不溶部分之间分布的研究表明,病毒粒子蛋白VP4、VP5和VP6的溶解程度远低于VP1和VP2。