Enzyme-Linked Immunosorbent Assay for an Octapeptide Based on a Genetically Engineered Fusion Protein

Allan Witkowski, Sylvia Daunert, Leonidas G. Bachas, Mark S. Kindy

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Traditional chemical means of preparing enzyme-ligand conjugates for use in enzyme-linked immunosorbent assays (ELISAs) lead to the production of multisubstituted enzyme-ligand conjugates with a high degree of variability in the site of ligand attachment. A genetically engineered fusion protein was prepared in order to investigate the feasibility of controlled production of conjugates for use in ELISAs. Specifically, a synthetic octapeptide was fused with bacterial alkaline phosphatase. The resulting enzyme-peptide conjugate is monosubstituted (one peptide per subunit), has a single site of attachment, and results in assays with good response characteristics. The use of such fusion proteins, which combine small analyte peptides with enzyme labels, can lead to a new approach to improved assays for numerous biomolecules, including peptide pharmaceuticals, neurotransmitters, hormones, cell surface antigens, etc.

Original languageEnglish (US)
Pages (from-to)1147-1151
Number of pages5
JournalAnalytical Chemistry
Volume65
Issue number9
DOIs
StatePublished - May 1 1993
Externally publishedYes

ASJC Scopus subject areas

  • Analytical Chemistry

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