ISSN:
1432-0991
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Abstract InEscherichia coli C infected with bacteriophage ϕX174, the cytoplasmic and outer membranes of the host bacterium exhibit various alterations in their protein composition as revealed by sodium dodecyl sulfate gel electrophoresis of purified membranes. These alterations result mainly from the action of the lysis gene product of the phage. One effect of the changes occurring in the membranes results in different rates of release of wild-type phage and its lysis-negative mutant from glycine spheroplasts. The activity of phospho-MurNAc-pentapeptide translocase, an enzyme involved in murein synthesis and located in the cytoplasmic membrane, is unimpaired by these alterations.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01566597
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