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Novel and sensitive noncompetitive enzyme immunoassay to measure peptides by biotinylation



Novel and sensitive noncompetitive enzyme immunoassay to measure peptides by biotinylation



Analytical Letters 22(2): 353-364



A novel and sensitive noncompetitive enzyme immunoassay for angiotensin I as a peptide model is described. Angiotensin I in buffer containing bovine serum albumin or in plasma was biotinylated using sulfosuccinimidyl-6-(biotinamido)hexanoate. The biotinylated angiotensin I was trapped onto anti-angiotensin I IgG-coated polystyrene balls and, after washing to eliminate other biotinylated substances, was eluted with HCl. The biotinylated angiotensin I eluted was reacted with anti-angiotensin I Fab'-peroxidase conjugate and trapped onto streptavidin-coated polystyrene balls. Peroxidase ac tivity bound to the polystyrene balls was assayed by fluorimetry. The detection limit of angiotensin I was 13 fg (10 amol)/tube and 6.5 ng/l of plasma, which was 10 to 480-fold lower than that previously reported by competitive radioimmunoassay and competitive enzyme immunoassay. And other peptides could also be measured more sensitively by the present method than by competitive radioimmunoassay.

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Accession: 007602584

Download citation: RISBibTeXText

DOI: 10.1080/00032718908052345


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