Enzyme-Linked Immunosorbent Assay of Fungal NADP+-Glutamate Dehydrogenase | Zendy

Francis L. Martin | Zendy; Bernard Botton | Zendy; Y Msatef | Zendy

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Enzyme-Linked Immunosorbent Assay of Fungal NADP⁺-Glutamate Dehydrogenase

Author(s) -

Francis L. Martin,

Bernard Botton,

Y Msatef

Publication year - 1983

Publication title -

plant physiology

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.72.2.398

Subject(s) - glutamate dehydrogenase , enzyme , biochemistry , alkaline phosphatase , substrate (aquarium) , dehydrogenase , chemistry , microbiology and biotechnology , lactate dehydrogenase , chromatography , biology , glutamate receptor , ecology , receptor

A sensitive and reliable method has been developed for the quantitation of NADP(+)-glutamate dehydrogenase from the phytopathogenic Ascomycete Sphaerostilbe repens using a two-step competitive enzyme-linked immunosorbent assay. Purified enzyme was adsorbed noncovalently to polystyrene wells and rabbit immunserum was allowed to bind to antigensensitized wells. Bound specific antibody was visualized by goat antirabbit immunoglobulin covalently linked to alkaline phosphatase using paranitrophenylphosphate as the substrate. Increasing amounts of purified enzyme or crude fungal extracts were quantitated by their ability to inhibit specific antibody adsorption to antigen-coated polystyrene wells. This system proves to be useful in the range of 10 to 80 nanograms of enzyme level. Using this assay, identical amounts of NADP(+)-glutamate dehydrogenase were found in mycelia grown on nitrate and ammonia sources.

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