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 | |
| Publication status | Published - 2003 Jan 1 |
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All Science Journal Classification (ASJC) codes
- Biotechnology
- Surfaces and Interfaces
- Physical and Theoretical Chemistry
- Colloid and Surface Chemistry
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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 journal › Article
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 -