還元型ニコチンアミドアデニンジヌクレオチドの酸化電流測定に基づく血清中のアスパラギン酸トランスアミナーゼ及びアラニントランスアミナーゼ活性の測定

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タイトル別名
  • Amperometric determination of the activities of aspartate aminotransferase and alanine aminotransferase based on the measurement of anodic current due to NADH.
  • カンゲンガタ ニコチンアミド アデニンジヌクレオチド ノ サンカ デンリュウ

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抄録

A dialysis membrane-covered plastic formed carbon electrode which has been newly developed produced reproducible steady-state currents due to the oxidation of NADH at potentials more positive than 0.2 V (vs. SCE). The limiting currents due to NADH were in the range of 0.30.5 V in solutions of pH 5 to 9 and proportional to the NADH concentration in the range of 2.5 to 1500 μM. The relative standard deviation for the measurement of limiting current due to 200 μM NADH was 2.6% for five runs. NADH reacts with oxaloacetate produced from aspartate by an aspartate aminotransferase (AST) catalyzed reaction in the presence of malate dehydrogenase (MD) and reacts with pyruvate produced from alanine by an alanine aminotransferase (ALT) catalyzed reaction in the presence of lactate dehydrogenase (LD). Based on the magnitude of the current due to 1 μM NADH being 0.17 nA, the activities of AST and ALT in serum were assayed by measuring the decrease in current due to NADH for five min in Tris buffer of pH 7.8 containing aspartate, 2-oxoglutarate and MD for AST assay and buffer of pH 7.5 containing alanine, 2-oxoglutarate and LD for ALT assay. The activities determined amperometrically for seventeen serum samples were in excellent agreement with those determined by the UV-enzymatic method. Correlation coefficients between the two sets of results were 0.996 for AST assay and 0.992 for ALT assay.

収録刊行物

  • 分析化学

    分析化学 43 (9), 709-714, 1994

    公益社団法人 日本分析化学会

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