Comparison of Luminescent Immunoassays Using Biotinylated Proteins of Aequorin, Alkaline Phosphatase and Horseradish Peroxidase as Reporters | Zendy

S Inouye | Zendy; Junichi Sato | Zendy

Open Access

Comparison of Luminescent Immunoassays Using Biotinylated Proteins of Aequorin, Alkaline Phosphatase and Horseradish Peroxidase as Reporters

Author(s) -

S Inouye,

Junichi Sato

Publication year - 2008

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.80524

Subject(s) - biotinylation , horseradish peroxidase , aequorin , chemistry , alkaline phosphatase , biochemistry , chromatography , peroxidase , microbiology and biotechnology , enzyme , biology , intracellular

We compare aequorin, alkaline phosphatase and horseradish peroxidase as reporters for luminescent immunoassays using alpha-fetoprotein (AFP) as a model analyte. Biotinylated aequorin was prepared from mutated aequorin containing a reactive cysteine residue by chemical conjugation. The measurable range of AFP using this biotinylated aequorin was 0.02-200 ng/ml, with a lower background level than the other biotinylated enzymes tested.

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