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Enzyme-Linked Immunosorbent Assay of Fungal NADP+-Glutamate Dehydrogenase 1

机译:真菌NADP +-谷氨酸脱氢酶1的酶联免疫吸附测定

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摘要

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.
机译:已开发出一种灵敏可靠的方法,采用两步竞争性酶联免疫吸附测定法从植物病原性子囊白粉菌中定量分析NADP +-谷氨酸脱氢酶。将纯化的酶非共价吸附到聚苯乙烯孔中,并使兔免疫血清与抗原致敏孔结合。使用对硝基苯磷酸酯作为底物,通过与碱性磷酸酶共价连接的山羊抗兔免疫球蛋白可视化结合的特异性抗体。通过其抑制特异性抗体吸附到抗原包被的聚苯乙烯孔中的能力来定量纯化的酶或粗制真菌提取物的量。事实证明,该系统在10到80纳克酶水平的范围内有用。使用该测定法,在硝酸盐和氨源上生长的菌丝体中发现了相同量的NADP +-谷氨酸脱氢酶。

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