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. 1969 Jan;111(1):7–15. doi: 10.1042/bj1110007

Purification, properties and mechanism of action of a staphylolytic enzyme produced by Aeromonas hydrophila

N W Coles 1, C M Gilbo 1, A J Broad 1
PMCID: PMC1187487  PMID: 5773751

Abstract

1. An enzyme produced by Aeromonas hydrophila and capable of lysing Staphylococcus aureus cells was purified 180-fold by gel filtration and chromatography on columns of AG-50 W resin. 2. Physical measurements on the purified enzyme suggest that it is a small basic protein with an isoelectric point between pH9·0 and pH9·5. 3. Maximum lytic activity was obtained in 20mm-tris–glycine buffer, pH8·5, at 45°, with no detectable activity in the absence of a nitrogenous base. 4. The enzyme is active in the above buffer containing 1·5m-sucrose, and is useful for the preparation of protoplasts of Staphylococcus aureus. 5. Purified cell wall peptidoglycans of two strains of Staphylococcus aureus, differing in amino acid composition, were hydrolysed by the enzyme with the liberation of glycine oligopeptides, principally diglycine and triglycine. 6. Synthetic glycine oligopeptides larger than triglycine, but not polyglycine, were hydrolysed, as were a number of leucine-containing dipeptides and tripeptides, but no proteolytic activity could be demonstrated. 7. It is concluded that the enzyme is lytic towards Staphylococcus aureus because it splits the pentaglycine cross-links of the cell-wall peptidoglycan.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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