Saccharomyces cerevisiad Quinone Reductase에 관한 연구 = A Study on the Quinone Reductase frmo Saccharomyces cerevisiae

국문 초록 (Abstract)

Saccharomyces cerevisiae로부터 quinone reductase를 정제하여 물리화학적 성질을 조사하였다. 정제된 효소는 polyacrylamide gel electrophoresis를 시행한 결과 하나의 주된 band를 나타내었고, gel filtration에 의해 측정된 이 효소의 분자량은 111,000 dalton 이었다. 또한 SDS-PAGE에 의해 측정된 subunit의 분자량은 22,000 dalton 이었고, 최적 pH는 6.0이었으며, 1,4-benzoquinone과 1,4-naphthoquinone에 대한 Km값은 각각 1.3M과 14.3?M인 것으로 나타났다.

다국어 초록 (Multilingual Abstract)

Quinone and related compounds have received considerable attention recently, due to their widespread environmental occurrence and toxicological potential.
Evidence has favored the hypothesis that quinone reductase is protective against quinone and quinone imine toxicity, by virtue of a two-electron reduction to the hydroquinone, thereby facilitating conjugation with glucuronide, partitioning into the aqueous phase, and excretion. In addition, it has been suggested that hepatic cytosolic quinone reductase has a functional role in ethanol metabolism and decreases hepatotoxicity. Furthermore, a water-soluble quinone, coenzyme Qo, was shown to stimulate insulin release, and it was suggested that quinone reductase might play some role in physiological insulin release.
An intracellular, soluble quinone reductase was purified from S. cerevisiae and some properties of the enzyme were examined. The enzyme exhibited a native molecular mass of approximately 111kDa as determined by gel filtration on a Sephacryl 200 column. The subunit molecular mass was estimated by SDS-PAGE to be 22kDa. The effect of pH on activity was measured with phosphate buffer. The optimum pH was shown to be pH 6.0. The apparent Km for 1,4-benzoquinone and 1,4-naphthoquinone are 1.3 mM and 14.3?M, respectively.

목차 (Table of Contents)

• Ⅰ. 서 론
• Ⅱ. 실험재료 및 방법
• Ⅲ. 결과 및 고찰
• 참고문헌
• Abstract