| Autor: |
Levashov PA; Faculty of Chemistry, Lomonosov Moscow State University, Moscow, 119991, Russia. levashov@aport.ru, Popov DV, Popova VM, Zhilenkov EL, Morozova OA, Belogurova NG, Sedov SA, Dyatlov IA, Klyachko NL, Levashov AV |
| Jazyk: |
angličtina |
| Zdroj: |
Biochemistry. Biokhimiia [Biochemistry (Mosc)] 2010 Sep; Vol. 75 (9), pp. 1160-4. |
| DOI: |
10.1134/s0006297910090105 |
| Abstrakt: |
Bacteriophage enzyme preparations exolysin and endolysin were studied. Exolysin (a phage-associated enzyme) was obtained from tail fraction and endolysin from phage-free cytoplasmic fraction of disintegrated Salmonella enteritidis cells. A new method for purification of these enzymes was developed, and their molecular masses were determined. The main catalytic properties of the studied enzymes (pH optimum and specificity to bacterial substrates) were found to be similar. Both enzymes lyse Escherichia coli cells like chicken egg lysozyme, but more efficiently lyse S. enteritidis cells and cannot lyse Micrococcus luteus, a good substrate for chicken egg lysozyme. Similar properties of exolysin and endolysin suggest that these enzymes are structurally similar or even identical. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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