DISSOCIATION OF THE LIPID-CONTAINING BACTERIOPHAGE-PRD1 - EFFECTS OF HEAT, PH, AND SODIUM DODECYL-SULFATE

被引:18
作者
CALDENTEY, J [1 ]
LUO, C [1 ]
BAMFORD, DH [1 ]
机构
[1] UNIV HELSINKI,INST BIOTECHNOL,SF-00100 HELSINKI 10,FINLAND
关键词
D O I
10.1006/viro.1993.1294
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The double-stranded DNA bacteriophage PRD1 replicates in Escherichia coli and Salmonella typhimurium. It has an outer protein coat surrounding a membrane. The phage lipids are derived from the host, but the membrane proteins are of phage origin. In this investigation we studied the effects of heat, pH, and sodium dodecyl sulfate on the integrity of phage particles. Heat and high pH result in the release of the main coat protein, P3, as trimers, whereas treatment of phage particles with detergent results in the solubilization of the membrane. Our results enable a distinction to be made between the phage structural proteins that are embedded in the lipid bilayer and those that appear to be more loosely associated with the membrane. © 1995 Academic Press Limited.
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页码:557 / 563
页数:7
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