Affiliation:
1. Department of Biochemistry, University of Chicago, Chicago, Illinois 60637
Abstract
Parallel studies have been made of the protein coats of the temperate bacteriophage λ and of a deletion mutant, λ virulent. A new method for preparing ghosts of both phages by the action of Cu
++
is described. Protein ghosts of both phages can be dissolved in citrate at
p
H values below 3, more rapidly in the presence of 8
m
urea. Both phages yielded three apparently identical protein components which can be separated by thin-layer gel filtration and thin-layer gel electrophoresis. The protein of molecular weight 47,000 ± 1,500 represents about 55% of the protein of the ghosts and is therefore likely to be the subunit of the head. The other proteins of molecular weight 30,000 ± 1,500 and 16,000 ± 1,500 represent approximately 25% and 20% of the protein, respectively. Amino acid analyses of the ghosts from the two phages have been carried out and show no significant differences. The buoyant density of phage λ virulent is 0.016 g/ml less than that of λ. Since no differences have been found in the protein components of the two phages, this indicates that the virulent mutant contains approximately 16% less deoxyribonucleic acid than the temperate phage.
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Cited by
16 articles.
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