Effects of surface characteristics on non-specific agglutination in latex immunoagglutination antibody assay

Jeong Yeol Yoon; Kyung Hee Kim; Sung Wook Choi; Jung Hyun Kim; Woo Sik Kim

doi:10.1016/S0927-7765(01)00211-9

Effects of surface characteristics on non-specific agglutination in latex immunoagglutination antibody assay

Jeong Yeol Yoon, Kyung Hee Kim, Sung Wook Choi, Jung Hyun Kim, Woo Sik Kim

Department of Chemical and Biomolecular Engineering

Research output: Contribution to journal › Article

12 Citations (Scopus)

Abstract

To monitor the non-specific agglutination (NSA) in latex immunoagglutination assay, antigen-coated structured latex particles, which have carboxyl and sulphonate groups as hydrophilic domains, were tested for an antibody assay. Sulphonated particles showed NSA in high antibody concentrations, where no surface antigen left to match with. This was further justified with the more stable highly sulphonated particles, which showed higher degree of NSA. It can therefore be confirmed that sulphonate groups cause (or at least promote) NSA, while carboxyl groups do not. Surface coverage over 17% was not fully utilized for antigen-antibody reaction, due to the prozone effect. The difference in sensitivity of particles was explained in terms of our new explanations on the governing interactions of protein adsorption.

Original language	English
Pages (from-to)	3-9
Number of pages	7
Journal	Colloids and Surfaces B: Biointerfaces
Volume	27
Issue number	1
DOIs	https://doi.org/10.1016/S0927-7765(01)00211-9
Publication status	Published - 2003 Jan 1

All Science Journal Classification (ASJC) codes

Biotechnology
Surfaces and Interfaces
Physical and Theoretical Chemistry
Colloid and Surface Chemistry

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Yoon, J. Y., Kim, K. H., Choi, S. W., Kim, J. H., & Kim, W. S. (2003). Effects of surface characteristics on non-specific agglutination in latex immunoagglutination antibody assay. Colloids and Surfaces B: Biointerfaces, 27(1), 3-9. https://doi.org/10.1016/S0927-7765(01)00211-9

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abstract = "To monitor the non-specific agglutination (NSA) in latex immunoagglutination assay, antigen-coated structured latex particles, which have carboxyl and sulphonate groups as hydrophilic domains, were tested for an antibody assay. Sulphonated particles showed NSA in high antibody concentrations, where no surface antigen left to match with. This was further justified with the more stable highly sulphonated particles, which showed higher degree of NSA. It can therefore be confirmed that sulphonate groups cause (or at least promote) NSA, while carboxyl groups do not. Surface coverage over 17% was not fully utilized for antigen-antibody reaction, due to the prozone effect. The difference in sensitivity of particles was explained in terms of our new explanations on the governing interactions of protein adsorption.",

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AU - Kim, Woo Sik

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