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Gewählte Publikation:

Krivanek, R; Rybar, P; Küpcü, S; Sleytr, UB; Hianik, T.
(2002): Affinity interactions on a liposome surface detected by ultrasound velocimetry.
Bioelectrochemistry. 2002; 55(1-2):57-59

Abstract:
In this work, we performed targeted immobilization of immunoglobulins by means of bacterial S-layer proteins from Bacillus coagulans E38-66/V1 recrystallized on liposomes, which were exploited as immobilization matrix for antibody (Ab)-human IgG. The study of interaction of rabbit or swine anti-human IgG as antigens (Ag) was performed by means of measuring changes of ultrasound velocity. We showed that at a temperature of 25 T, the increment of ultrasound velocity [u] linearly decreased following an increase of concentration of Ag. The decrease of [u] was presumably due to changes of hydration of the membrane due to the binding process. Approximately 10 times lower changes of [u] were observed at 45 degreesC for Ag-Ab interaction as well as for nonspecific interaction of Ag with liposomes covered by Slayer without Ab. No substantial differences in the behaviour of [u] were observed for interactions of human IgG with rabbit or swine antihuman IgG. (C) 2002 Elsevier Science B.V. All rights reserved.
Autor*innen der BOKU Wien:
Küpcü Seta
Sleytr Uwe B.
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Bacterial Proteins - metabolism
Densitometry - metabolism
Humans - metabolism
Immunoglobulin G - metabolism
Liposomes - metabolism
Ultrasonics - metabolism

Find related publications in this database (Keywords)
IgG
S-layer
liposomes
hydration
ultrasound velocimetry
densitometry


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