Send to

Choose Destination
Enzyme Microb Technol. 2000 Mar 1;26(5-6):451-458.

Critical evaluation of p-nitrophenylphosphorylcholine (p-NPPC) as artificial substrate for the detection of phospholipase C*

Author information

Abteilung für Transfusionsmedizin, Universitätsklinikum Tübingen, Hoppe-Seyler-Str. 3, D-72076, Tübingen, Germany


Phospholipase C (PLC) activity secreted by bacteria as a virulence factor is commonly detected by use of the artificial substrate p-nitrophenylphosphorylcholine (p-NPPC). We examined several commercially available enzymes (phosphodiesterases, phosphomonoesterases, phospholipase A, lipase, protease) for their hydrolytic activity towards p-NPPC and compared these results with those of PLC tests using phospholipid substrates. Our data indicate that, in addition to PLC, several other enzymes which can affect phosphate esters are able to hydrolyze p-NPPC. We therefore suggest to use lipid substrates for correct characterization of bacterial PLCs, especially when whole bacteria or crude enzyme preparations are investigated.


Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center