Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1934198 | Biochemical and Biophysical Research Communications | 2008 | 4 Pages |
Abstract
The lysozyme of bacteriophage φIN93 was purified to apparent homogeneity with Carboxymethyl Sepharose and Hydroxyapatie columns from lysates of the phage grown on Thermus aquaticus TZ2. The enzyme is a single polypeptide chain with a molecular weight of 33,000. From the determined N-terminal amio acids of the enzyme, the locus of the gene was specified on a φIN93 genome. The enzyme was not similar to egg white lysozyme, T4 phage lysozyme, or lambda phage lysozyme. The enzyme, φIN93 lysozyme, was found to be a novel type of thermophilic lysozyme, which lyses specifically Thermus sp. cells, and exhibited conspicuous thermal stability at 95 °C for 1 h in the presence of β-mercaptoethanol.
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Authors
Isao Matsushita, Hideshi Yanase,