High-pressure-mediated dissociation of immune complexes demonstrated in model systems

Autor:	James A. Laugharn, Charles Y. Cheung, Litt Gerald J, David J. Green
Rok vydání:	1998
Předmět:	biology Molecular model Stereochemistry Chemistry Biochemistry (medical) Clinical Biochemistry Hydrostatic pressure Immune complex Dissociation (chemistry) Immune system Antigen High pressure biology.protein Biophysics Antibody
Zdroj:	Clinical Chemistry. 44:299-303
ISSN:	1530-8561 0009-9147
DOI:	10.1093/clinchem/44.2.299
Popis:	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.
Databáze:	OpenAIRE
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