Modified Listeria bacteriophage lysin genes (ply) allow efficient overexpression and one-step purification of biochemically active fusion proteins.
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ABSTRACT:
SUBMITTER: Loessner MJ
PROVIDER: S-EPMC168095 | biostudies-other | 1996 Aug
REPOSITORIES: biostudies-other
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Modified Listeria bacteriophage lysin genes (ply) allow efficient overexpression and one-step purification of biochemically active fusion proteins.
Loessner M J MJ Schneider A A Scherer S S
Applied and environmental microbiology 19960801 8
Listeria bacteriophage lytic enzymes are useful for in vitro applications such as rapid, gentle cell disruption, and they provide new approaches as selective antimicrobial agents for destruction of Listeria monocytogenes in contaminated foods. We describe here the amino-terminal modification of three cloned Listeria phage lysin genes (ply), resulting in fusion proteins with a 12-amino-acid leader containing six consecutive histidine residues. The recombinant enzymes retain their native specific ...[more]
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