Characterization of a human pancreatic secretory trypsin inhibitor mutant binding to Legionella pneumophila as determined by a quartz crystal microbalance
J. Decker et al., Characterization of a human pancreatic secretory trypsin inhibitor mutant binding to Legionella pneumophila as determined by a quartz crystal microbalance, J IMMUNOL M, 233(1-2), 2000, pp. 159-165
We describe the isolation from a large phagemid library of a human pancreat
ic secretory trypsin inhibitor (hPSTI) mutant that binds to Legionella pneu
mophila. To gain further insight into the binding kinetics of the isolated
hPSTI mutant, an immunosensing system based on a quartz crystal microbalanc
e (QCM) was used. In contrast to ELISA procedures, k(on) and k(off) rates c
ould be derived from the QCM sensograms. Thus, it is possible to characteri
ze specific intermolecular interactions between proteins and phages isolate
d from large phage display libraries by QCM. (C) 2000 Elsevier Science B.V.
All rights reserved.