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

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

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 (US)
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
State	Published - Jan 1 2003
Externally published	Yes

Keywords

Anti-BSA
Anti-bovine serum albumin
LAT
Latex agglutination test
Latex immunoagglutination assay
Non-specific agglutination

ASJC Scopus subject areas

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

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10.1016/S0927-7765(01)00211-9

Cite this

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title = "Effects of surface characteristics on non-specific agglutination in latex immunoagglutination antibody assay",

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.",

keywords = "Anti-BSA, Anti-bovine serum albumin, LAT, Latex agglutination test, Latex immunoagglutination assay, Non-specific agglutination",

author = "Yoon, {Jeong Yeol} and Kim, {Kyung Hee} and Choi, {Sung Wook} and Kim, {Jung Hyun} and Kim, {Woo Sik}",

note = "Funding Information: Funding for this research was provided by the Bioproduct Research Center of Yonsei University, and the Korea Institute of S&T Evaluation and Planning (National Research Laboratory Program, 2000-N-NL-01-C-032).",

year = "2003",

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day = "1",

doi = "10.1016/S0927-7765(01)00211-9",

language = "English (US)",

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journal = "Colloids and Surfaces B: Biointerfaces",

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T1 - Effects of surface characteristics on non-specific agglutination in latex immunoagglutination antibody assay

AU - Yoon, Jeong Yeol

AU - Kim, Kyung Hee

AU - Choi, Sung Wook

AU - Kim, Jung Hyun

AU - Kim, Woo Sik

N1 - Funding Information: Funding for this research was provided by the Bioproduct Research Center of Yonsei University, and the Korea Institute of S&T Evaluation and Planning (National Research Laboratory Program, 2000-N-NL-01-C-032).

PY - 2003/1/1

Y1 - 2003/1/1

N2 - 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.

AB - 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.

KW - Anti-BSA

KW - Anti-bovine serum albumin

KW - LAT

KW - Latex agglutination test

KW - Latex immunoagglutination assay

KW - Non-specific agglutination

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DO - 10.1016/S0927-7765(01)00211-9

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SN - 0927-7765

VL - 27

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JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

IS - 1

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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