STRUCTURAL PROTEINS OF ADENOVIRUSES .10. ISOLATION AND TOPOGRAPHY OF LOW-MOLECULAR WEIGHT ANTIGENS FROM VIRION OF ADENOVIRUS TYPE-2
STRUCTURAL PROTEINS OF ADENOVIRUSES .10. ISOLATION AND TOPOGRAPHY OF LOW-MOLECULAR WEIGHT ANTIGENS FROM VIRION OF ADENOVIRUS TYPE-2
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DOI：
10.1016/0042-6822(73)90404-2
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发表时间：
1973-01-01
期刊：
影响因子：
3.7
通讯作者：
PHILIPSON, L
中科院分区：
文献类型：
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作者：
EVERITT, E;SUNDQUIST, B;PHILIPSON, L
利用高分辨率SDS-聚丙烯酰胺凝胶电泳（Maizel，1971）和提取碱性蛋白的新方法，确定2型腺病毒含有至少10种不同的多肽（II、III、IIIa、IV-X），并且可能更多。五种蛋白质（V，VI，VII，VIII和X）进行了纯化，通过在尿素中选择性提取在高离子强度，低pH值，然后制备聚丙烯酰胺电泳向阴极在pH 3.4。使用针对蛋白质V、VI和VII产生的抗血清来揭示这些蛋白质在抗原性上是不同的并且与六邻体、五邻体和纤维无关。1970年）。多肽V和VII与含DNA的核心相关。多肽VI似乎与病毒体的所有六邻体相关。除了多肽II和VI、多肽IX以及可能的多肽VIII之外，还含有来自衣壳的三角形小平面的六邻体。从感染细胞纯化的六邻体仅含有多肽II。多肽IIIa优先与周五醛六邻体一起释放。
With high resolution SDS-polyacrylamide gel electrophoresis (Maizel, 1971) and a new method to extract the basic proteins, it was ascertained that adenovirus type 2 contains at least 10 distinct polypeptides (II, III, IIIa, IV–X) and possibly more. Five proteins (V, VI, VII, VIII, and X) were purified by selective extraction in urea at high ionic strength, and low pH followed by preparative polyacrylamide electrophoresis toward the cathode at pH 3.4. Antisera, produced against proteins V, VI, and VII were used to reveal that these proteins were antigenically distinct and unrelated to hexons, pentons, and fibers.The location of the polypeptides was investigated by two methods of virion degradation (Prageet al., 1970). Polypeptides V and VII were associated with the DNA-containing core. Polypeptide VI appeared to be associated with all hexons of the virion. Hexons from the triangular facets of the capsid contained in addition to polypeptides II and VI, polypeptide IX, and possibly also polypeptide VIII. Hexons purified from infected cells contained only polypeptide II. Polypeptide IIIa was preferentially released together with the peripentonal hexons.