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 journalArticle

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 languageEnglish
Pages (from-to)3-9
Number of pages7
JournalColloids and Surfaces B: Biointerfaces
Volume27
Issue number1
DOIs
Publication statusPublished - 2003 Jan 1

Fingerprint

agglutination
Agglutination
Latex
Antigens
latex
Latexes
antibodies
Antibodies
Assays
antigens
Antigen-antibody reactions
carboxyl group
Surface Antigens
sulfonates
Particles (particulate matter)
Antigen-Antibody Reactions
Proteins
Adsorption
Microspheres
proteins

All Science Journal Classification (ASJC) codes

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

Cite this

Yoon, Jeong Yeol ; Kim, Kyung Hee ; Choi, Sung Wook ; Kim, Jung-Hyun ; Kim, Woo Sik. / Effects of surface characteristics on non-specific agglutination in latex immunoagglutination antibody assay. In: Colloids and Surfaces B: Biointerfaces. 2003 ; Vol. 27, No. 1. pp. 3-9.
@article{ddb62170ccaa49a9bfce94da12a981a4,
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.",
author = "Yoon, {Jeong Yeol} and Kim, {Kyung Hee} and Choi, {Sung Wook} and Jung-Hyun Kim and Kim, {Woo Sik}",
year = "2003",
month = "1",
day = "1",
doi = "10.1016/S0927-7765(01)00211-9",
language = "English",
volume = "27",
pages = "3--9",
journal = "Colloids and Surfaces B: Biointerfaces",
issn = "0927-7765",
publisher = "Elsevier",
number = "1",

}

Effects of surface characteristics on non-specific agglutination in latex immunoagglutination antibody assay. / Yoon, Jeong Yeol; Kim, Kyung Hee; Choi, Sung Wook; Kim, Jung-Hyun; Kim, Woo Sik.

In: Colloids and Surfaces B: Biointerfaces, Vol. 27, No. 1, 01.01.2003, p. 3-9.

Research output: Contribution to journalArticle

TY - JOUR

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

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.

UR - http://www.scopus.com/inward/record.url?scp=0037210378&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037210378&partnerID=8YFLogxK

U2 - 10.1016/S0927-7765(01)00211-9

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

M3 - Article

AN - SCOPUS:0037210378

VL - 27

SP - 3

EP - 9

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

SN - 0927-7765

IS - 1

ER -