Abstract
A factor which inactivates the phage lambda can be extracted from Escherichia coli. This factor is a protein and is located in the outer membrane of the bacterial envelope. It is found in extracts of strains which are sensitive to phage lambda, but not in extracts of strains specifically resistant to this phage. We conclude that this factor is the lambda receptor, responsible for the specific adsorption of the phage lambda to E. coli cells. A partial purification of the lambda receptor is described. Inactivation of the phage by purified receptor is shown to be accompanied by the release of deoxyribonucleic acid from the phage.
MeSH Terms
Adsorption
Bacterial Proteins/isolation & purification,pharmacology
Carbon Radioisotopes
Cell Wall/analysis
Chemical Precipitation
Chloroform
Cholic Acids
Chromatography
Coliphages/drug effects
DNA, Viral
Edetic Acid
Electrophoresis, Polyacrylamide Gel
Escherichia coli/analysis,cytology
Lysogeny
Methanol
Microscopy, Electron
Mutation
Receptors, Drug
Tritium
Ultracentrifugation
Chemicals
Bacterial Proteins
Carbon Radioisotopes
Cholic Acids
DNA, Viral
Receptors, Drug
Tritium
Chloroform
Edetic Acid
Methanol
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Randall-Hazelbauer L
Schwartz M
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