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Comparison of the Biophysical and Biochemical Properties of Penicillium cyaneo-fulvum Virus and Penicillium chrysogenum Virus

衣壳 产黄青霉 生物 核糖核酸 类病毒颗粒 病毒 聚丙烯酰胺凝胶电泳 凝胶电泳 电泳 分子质量 大小排阻色谱法 分子生物学 生物化学 病毒学 基因 重组DNA
作者
K. W. Buck,R. F. Girvan
出处
期刊:Journal of General Virology [Microbiology Society]
卷期号:34 (1): 145-154 被引量:29
标识
DOI:10.1099/0022-1317-34-1-145
摘要

SUMMARY The biophysical and biochemical properties of Penicillium cyaneo-fulvum virus (Pc-fV) and Penicillium chrysogenum virus (PcV) have been compared. In sucrose density gradient sedimentation, purified virus preparations gave one major component, L, and three minor components E1, E2 and H with sedimentation coefficients of 145S, 80S, 102S and 172S respectively in each case. E1, E2 were shown to be empty particles. Pc-fV L particles contained only double-stranded RNA, which separated in polyacrylamide gel electrophoresis into four components with mol. wt. 2.21 × 106, 2.08 × 106, 1.98 × 106 and 1.93 × 106. PcV L particles gave three double-stranded RNA components, which were indistinguishable in polyacrylamide gel electrophoresis from the larger three RNA components of Pc-fV. In both viruses each RNA component was separately encapsidated. In both viruses H particles gave rise to the same double-stranded RNA components as their L particles, but contained, in addition, small amounts of single-stranded RNA. Pc-fV and PcV have been shown to consist of isometric particles of the same size and to be serologically related, and the amino acid compositions of their capsid polypeptides were found to be very similar. The capsid polypeptides of the two viruses were examined by SDS-polyacrylamide gel electrophoresis. In each case E2, L and H particles gave one major polypeptide λ1, with mol. wt. 130000, whereas E1 particles contained one major polypeptide λ2 with mol. wt. 115000. The mol. wt. of L particles, determined from sedimentation and diffusion coefficients, was 9.8 × 106 for both Pc-fV and PcV. The capsid of the L particles of each virus was estimated to contain 60 molecules of polypeptide λ1.
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