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Abstract
Preparation and purification of a recombinant protein are described along with characteristics of its specific (for -([gamma]-Glu)-Lys and D-dimer substrates) and nonspecific (for L-[gamma]-Glu-pNA) isopeptidase activities; the absence of peptidase function for [alpha]-([alpha]-Glu)-Lys substrate is noted. It is shown that the protein exhibits muramidase (cell walls of Micrococcus lysodeikticus) and specific glycosidase activities. The latter was determined towards the fluorogenic substrate 4-methylum-belliferyl-tetra-N-acetyl-[beta]-chitotetraoxide. Antimicrobial activity of recombinant destabilase-lysozyme protein (recDest-Lys) and its 11-membered amphipathic peptide was revealed towards cells of the strict anaerobic Archaean Methanosarcina barkeri, whose cell walls contain no murein. Possible mechanisms of the effect of recDest-Lys on these cells are discussed. [PUBLICATION ABSTRACT]