Partial purification and some properties of phi C2(W) lysin, a lytic enzyme produced by phage-infected cells of Streptococcus lactis C2. 1985

W M Mullan, and R J Crawford

The lytic enzyme present in phi C2(W) lysates was isolated by means of ion-exchange chromatography and further purified by gel filtration and ultrafiltration. The phage enzyme had an apparent pH optimum of 6.5-6.9 and was rapidly inactivated at temperatures greater than 47 degrees C. The apparent temperature optimum was 37 degrees C and Q10 and Ea values over the range 22-32 degrees C were 2.5 and 69.2 kJ/mol respectively. Monovalent and divalent cations activated the enzyme. Reduced -SH groups on the enzyme were required for lytic activity. Gel filtration revealed a mol. wt of approximately 46000. Strain-dependent differences in sensitivity of group N lactic streptococci to lysin were found. Group D streptococci were also lysed. Strains of three species of Leuconostoc, two species of Lactobacillus, one strain of Escherichia coli and of Micrococcus lysodeikticus were apparently resistant. Analysis of cell wall degradation products gave results which were consistent with the lysin having the specificity of an N-acetylmuramidase.

UI MeSH Term Description Entries
D008242 Lysogeny The phenomenon by which a temperate phage incorporates itself into the DNA of a bacterial host, establishing a kind of symbiotic relation between PROPHAGE and bacterium which results in the perpetuation of the prophage in all the descendants of the bacterium. Upon induction (VIRUS ACTIVATION) by various agents, such as ultraviolet radiation, the phage is released, which then becomes virulent and lyses the bacterium. Integration, Prophage,Prophage Integration,Integrations, Prophage,Prophage Integrations
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D002473 Cell Wall The outermost layer of a cell in most PLANTS; BACTERIA; FUNGI; and ALGAE. The cell wall is usually a rigid structure that lies external to the CELL MEMBRANE, and provides a protective barrier against physical or chemical agents. Cell Walls,Wall, Cell,Walls, Cell
D004798 Enzymes Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified. Biocatalyst,Enzyme,Biocatalysts
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D001435 Bacteriophages Viruses whose hosts are bacterial cells. Phages,Bacteriophage,Phage
D013294 Lactococcus lactis A non-pathogenic species of LACTOCOCCUS found in DAIRY PRODUCTS and responsible for the souring of MILK and the production of LACTIC ACID. Streptococcus lactis,Lactococcus lactis subsp. lactis
D014764 Viral Proteins Proteins found in any species of virus. Gene Products, Viral,Viral Gene Products,Viral Gene Proteins,Viral Protein,Protein, Viral,Proteins, Viral
D014776 Virus Cultivation Process of growing viruses in live animals, plants, or cultured cells. Viral Cultivation,Cultivation, Viral,Cultivation, Virus,Cultivations, Viral,Cultivations, Virus,Viral Cultivations,Virus Cultivations

Related Publications

W M Mullan, and R J Crawford
September 1992, Biochimica et biophysica acta,
W M Mullan, and R J Crawford
January 1975, Nihon saikingaku zasshi. Japanese journal of bacteriology,
W M Mullan, and R J Crawford
October 1958, Canadian journal of microbiology,
W M Mullan, and R J Crawford
June 1989, Hiroshima Daigaku shigaku zasshi. The Journal of Hiroshima University Dental Society,
W M Mullan, and R J Crawford
February 1987, Proceedings of the National Academy of Sciences of the United States of America,
W M Mullan, and R J Crawford
April 2012, World journal of microbiology & biotechnology,
W M Mullan, and R J Crawford
January 1978, European journal of biochemistry,
Copied contents to your clipboard!