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 Scopus citations


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



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

ASJC Scopus subject areas

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

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