Premium
Bactericidal activities of lysozyme and aprotinin against Gram‐negative and Gram‐positive bacteria related to their basic character
Author(s) -
Pellegrini A.,
Thomas U.,
Fellenberg R.,
Wild P.
Publication year - 1992
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1992.tb01821.x
Subject(s) - lysozyme , aprotinin , gram negative bacteria , muramidase , chemistry , bacteria , egg white , biochemistry , microbiology and biotechnology , escherichia coli , dithiothreitol , gram positive bacteria , enzyme , biology , medicine , surgery , gene , antibiotics , genetics
A. PELLEGRINI, U. THOMAS, R. VON FELLENBERG AND P. WILD. 1992. Bactericidal properties of aprotinin, a proteinase inhibitor and possibly a defence molecule in bovine species, and of chicken egg white lysozyme, known as muramidase, were investigated. Incubation of various bacteria in the presence of either aprotinin or lysozyme showed that both proteins killed Gram‐positive as well as Gram‐negative bacteria without addition of complement or EDTA. Denaturation of the two proteins by dithiothreitol did not lead to loss of their bactericidal potency. Electron microscopic examination of Escherichia coli incubated either with lysozyme or aprotinin revealed that the bacterial cytoplasms gradually disintegrated. Both aprotinin and lysozyme were demonstrated within the affected cytoplasm by immunogold labelling. The results suggest that the bactericidal potency of lysozyme is not only due to muramidase activity but also to its cationic and hydrophobic properties. The bactericidal activity of aprotinin is probably also related to both these properties rather than to its activity as proteinase inhibitor.