Development of activity-based probes for trypsin-family serine proteases.
A series of diphenylphosphonate-based probes were developed for the trypsin-like serine proteases. These probes selectively target serine proteases rather than general serine hydrolases that are targets for fluorophosphonate-based probes. This increased selectivity allows detection of low abundance serine proteases in complex proteomes using simple SDS-PAGE methods. We present here the application of multiple probes in enzyme activity profiling of intact mast cells, a type of inflammatory cell implicated in allergy and autoimmune diseases.
Pan
Zhengying
Z
Celera Genomics, 180 Kimball Way, South San Francisco, CA 94080, USA. zypan@yahoo.com
Jeffery
Douglas A
DA
Chehade
Kareem
K
Beltman
Jerlyn
J
Clark
James M
JM
Grothaus
Paul
P
Bogyo
Matthew
M
Baruch
Amos
A
D002460:Cell Line; D006801:Humans; D008407:Mast Cells / Q000187:drug effects / Q000201:enzymology; D015394:Molecular Structure; D014357:Trypsin / Q000145:classification* / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*
D014361:Trypsin Inhibitors; D014357:Trypsin