(Clinical Chemistry. 1998;44:299-303.)
© 1998 American Association for Clinical Chemistry, Inc.
High-pressure-mediated dissociation of immune complexes demonstrated in model systems
Charles Y. Cheung,
David J. Green,
Gerald J. Litt,
and James A. Laugharn, Jr.a
a Author for correspondence. Fax 617-932-8705; e-mail jlaugharn{at}bioseq.com.
The use of pressure to disrupt immune complexes was demonstrated in two
model systems: prostate-specific antigen (PSA) and anti-PSA antibody;
and epiglycanin, a mucin glycoprotein, and an antibody specific to that
protein. Dissociation of the anti-PSA antibody from the immobilized PSA
antigen was observed when pressures of 415 MPa and 550 MPa (1 MPa
~144 psi) were applied at room temperature (~21 °C). Application
of pressures ranging from 140 MPa to 550 MPa resulted in dissociation
of antibody from epiglycanin. In both cases, the rebinding of
dissociated antibody to immobilized antigen indicated that the effect
of high pressure on the binding of the immune complexes was reversible.
These findings suggest that application of high hydrostatic pressure
has the potential to be used to significantly improve the sensitivity
and specificity of clinical assays.
