May 17, 1976

Enzymic and molecular properties of base-plate parts of bacteriophage P22

European Journal of Biochemistry
S Iwashita, S Kanegasaki

Abstract

Using 14C-labeled Salmonella bacterial cells as the substrate, the enzymic and molecular properties of the base-plate parts of phage P22 were studied. The base-plate part consisted of a single protein species which cleaved extensively the O-antigen of Salmonella typhimurium, Salmonelly schottmuellerie and with somewhat slower rate that of Salmonella typhi, releasing oligo-saccharide products with rhamnose at the reducing end. Much less cleavage was observed with a strain of S. typhimurium lysogenic for P22, and no significant reaction with Salmonella anatum, Salmonella newington and Salmonella minneapolis. The base-plate part enzyme was a very heat-stable protein and only 10-20% loss was observed after treatment at 85 degrees C for 5 min. The pH optimum of the enzyme was around 7.5, and the glycosidase activity was not influenced by the ionic strength (25-250 mM( of the medium or the presence of Mg2+. The molecular weight of the base-plate part was 320,000 by sedimentation equilibrium. Dodecylsulphate-acrylamide gel electrophoresis revealed a single band of molecular weight 77,000, indicating that a single base-plate part corresponds to a tetramer of identical subunits. Circular dichroism spectra of P22 base-plate parts showed ...Continue Reading

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  • Citations34

Mentioned in this Paper

Acrylamide
Glycosidase Activity
Salmonella typhi
Amino Acids, I.V. solution additive
Viral Proteins
Peptide Hydrolases
Bacteriophage P22
Cytokinesis of the Fertilized Ovum
Glycine
Glycine (Plant)

About this Paper

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