UNASSIGNED: Isoenzyme c of horseradish peroxidase (HRP-C) is widely used in enzyme immunoassay combined with chemiluminescence (CL) detection. For this application, HRP-C activity measurement is usually based on @entity6931 oxidation in the presence of @entity273 ( @entity5568 ). However, this catalysis reaction was enhancer dependent. In this study, we demonstrated that @entity21521 peroxidase (JcGP1) showed high efficiency in catalyzing @entity6931 oxidation in the presence of @entity5568 . Compared with HRP-C, the JcGP1-induced reaction was enhancer independent, which made the enzyme-linked immunosorbent assay (ELISA) simpler. In addition, the JcGP1 catalyzed reaction showed a long-term stable CL signal. We optimized the conditions for JcGP1 catalysis and determined the favorable conditions as follows: 50 mM Tris buffer (pH 8.2) containing 10 mM @entity5568 , 14 mM @entity6931 and 0.75 M @entity4202 . The optimum catalysis temperature was 30  C. The detection limit of JcGP1 under optimum condition was 0.2 pM. Long-term stable CL signal combined with enhancer-independent property indicated that JcGP1 might be a valuable candidate peroxidase for clinical diagnosis and enzyme immunoassay with CL detection. Copyright    2014 John Wiley _ Sons, Ltd.

Long-term chemiluminescence signal is produced in the course of XXXX oxidation catalyzed by enhancer-independent peroxidase purified from @entity21521 leaves.

@entity5568 :: ('D006861', 'Chemical') :: ['H2 O2'] @entity21521 :: ('180498', 'Species') :: ['Jatropha curcas'] @entity6931 :: ('MESH:D008165', 'Chemical') :: ['luminol'] @entity273 :: ('MESH:D006861', 'Chemical') :: ['hydrogen peroxide'] @entity4202 :: ('D012965', 'Chemical') :: ['NaCl']
@entity6931 :: (MESH:D008165,Chemical) :: ['luminol']
