Lytic sensitivity of Actinobacillus actinomycetemcomitans Y4 to lysozyme.
Abstract
The ability of both human and hen egg white lysozymes to lyse Actinobacillus actinomycetemcomitans Y4 was investigated. Lysis was followed optically at 540 nm by measuring the percent reduction in turbidity of freshly harvested log-phase cells suspended in Tris-maleate buffers within a wide range of pH (5.2 to 8.5) and molarity (0.01 to 0.2 M) and containing various amounts of enzyme and EDTA. In several instances, treated microorganisms were subsequently examined in thin sections by electron microscopy. Reductions in turbidity and clearing of suspensions occurred with small amounts of lysozyme (less than 1 microgram) under relatively alkaline conditions and at low ionic strength and in the presence of small amounts of EDTA (greater than 0.01 mM). Under the most alkaline conditions, EDTA alone effected turbidity reductions similar to those observed in the presence of lysozyme, which suggested that EDTA not only increased outer membrane permeability but also caused cell lysis. Ultrastructural analysis did not always correspond to turbidimetric observations. Cell lysis was virtually complete in suspensions containing both lysozyme and EDTA. However, in contrast to turbidimetric findings, a significant percentage of cells (greater...Continue Reading
References
Protein-lipopolysaccharide interactions. 1. The reaction of lysozyme with Pseudomonas aeruginosa LPS
Tris(hydroxymethyl)aminomethane buffer modification of Escherichia coli outer membrane permeability.
Citations
The in vitro lysozyme susceptibility of Candida albicans cultured in carbohydrate-supplemented media
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