TY  - JOUR
TI  - Activity Assays for Bacteriophage Endolysin PlyPy
AU  - Lood, Rolf  
AU  - Fischetti, Vincent  A. 
VL  - 4
IS  - 18
PY  - 2014
DA  - 2014/09/20
SP  - e1233
C1  - Bio-protocol 2014;4:e1233
DO  - 10.21769/BioProtoc.1233
UR  - https://doi.org/10.21769/BioProtoc.1233
AB  - Bacterial viruses (bacteriophages) escape and kill their host by degrading the bacterial peptidoglycan layer through the mechanism of enzymes called endolysins: peptidoglycan degrading enzymes. The method included here is useful for the initial characterization of any endolysin, regardless of the specific catalytic domain (as long as the activity results in a reduction in the optical density), in order to determine its optimal enzymatic (lytic) activity. This protocol is specific for the Streptococcus pyogenes phage endolysin PlyPy, but can be adapted for any peptidoglycan degrading enzyme.
KW  - Phage lysins
KW  - Lysis
KW  - Lytic activity
KW  - Cell wall hydrolase
KW  - Peptidoglycan cleavage
JF  - Bio-protocol
SN  - 2331-8325
PB  - Bio-protocol LLC.
BIO101  - False