Back to Search
Start Over
Enzymic and Molecular Properties of Base-Plate Parts of Bacteriophage P22.
- Source :
- European Journal of Biochemistry; May76 Part 2, Vol. 65 Issue 1, p87-94, 8p
- Publication Year :
- 1976
-
Abstract
- Using <superscript>14</superscript>C-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 oligosaccharide products with rhamnose at the reducing end. Much less cleavage was observed with a strain of S. typhimurium lysogenie 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 °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 Mg<superscript>2+</superscript>. The molecular weight of the base-plate part was 320000 by sedimentation equilibrium. Dodecylsulphate-acrylamide gel electrophoresis revealed a single band of molecular weight 77000, indicating that a single base-plate part corresponds to a tetramer of identical subunits. Circular dichroism spectra of P22 base-plate parts showed a major contribution of β structure. The protein was rich in acidic amino acids, glycine and serine. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 65
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13490737
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1976.tb10392.x