Antibody immobilisation on the metal and silicon surfaces. The use of self-assembled layers and specific receptors

STARODUB, N. F., PIROGOVA, L. V., DEMCHENKO, A. and NABOK, A. V. (2005). Antibody immobilisation on the metal and silicon surfaces. The use of self-assembled layers and specific receptors. Bioelectrochemistry, 66 (1-2), 111-115.

Full text not available from this repository.

Abstract

The use of Staplylococcal protein A and lectins as intermediate immobilising agents allows operators to orient antibodies (Ab) towards the solution due to the presence of a specific binding sites of immunoglobulin (Ig) molecules. Antibodies of different species of animals have unequal affinities to individual lectins. The effective thickness of immobilised Ab's depends on the type of substrates used and increases in the following sequence: bare gold or silicon surface, the surface treated with self-assembled polyelectrolytes (PESA) or with protein A or some lectins deposited on the preliminary formed polyelectrolyte layer. The glycolysated protein of jp51 may be selectively immobilised from the mixture of retroviral proteins (p24 and jp51), if it is necessary to distinguish infected animals from preliminarily immunised ones by means of a vaccine based on p24 protein. It was shown that the use of Staphylococcal protein A, instead of some lectins as intermediate layer for the Ab immobilisation. does not lead to a more sensitive determination of such low-weight toxins as 2,4-dichlorophenoxyacetic acid (2,4D). The above-mentioned results were obtained with surface plasmon resonance (SPR) technique. (c) 2004 Elsevier B.V. All rights reserved.

Item Type:	Article
Additional Information:	International Workshop on Surface Modification for Chemical and Biochemical Sensing, NOV 13-16, 2003 Bialowieza, POLAND Sp. Iss. SI
Research Institute, Centre or Group - Does NOT include content added after October 2018:	Materials and Engineering Research Institute > Advanced Coatings and Composites Research Centre > Electronic Materials and Sensors Research Group
Identification Number:	https://doi.org/10.1016/j.bioelechem.2004.04.007
Page Range:	111-115
Depositing User:	Ann Betterton
Date Deposited:	30 Mar 2010 16:12
Last Modified:	18 Mar 2021 21:30
URI:	https://shura.shu.ac.uk/id/eprint/1451

Actions (login required)

View Item

Downloads

Publication Metrics