A NOVEL UBIQUINONE REDUCTASE-ACTIVITY IN RAT CYTOSOL

被引:32
作者
TAKAHASHI, T
SHITASHIGE, M
OKAMOTO, T
KISHI, T
GOSHIMA, K
机构
[1] KOBE GAKUIN UNIV,FAC PHARMACEUT SCI,NISHI KU,KOBE 65121,JAPAN
[2] KOBE GAKUIN UNIV,FAC HUMANITIES & SCI,NISHI KU,KOBE 65121,JAPAN
关键词
NAD(P)H; DT-DIAPHORASE; CYTOSOL (RAT LIVER); UBIQUINONE REDUCTASE; SUBCELLULAR ORGANELLE;
D O I
10.1016/0014-5793(92)81499-C
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ubiquinone (UQ) reductase activity which reduces UQ to ubiquinol (UQH2) in rat tissues was roughly proportional to the UQH2/total UQ ratio in respective tissues. The highest activity was found in the liver, showing the highest UQH2/total UQ ratio. A greater part of liver UQ reductase activity was located in the cytosol. Within a week, the liver UQ reductase activity decreased by 80% even at -20-degrees-C. The DT-diaphorase activity was stable. UQ reductase required NADPH as the hydrogen donor and was not inhibited by a less than 1 muM concentration of dicoumarol. There was no stimulation of UQ reductase in the presence of bovine serum albumin nor in Triton X-100. Yet, both stimulated DT-diaphorase. As a result, UQ reductase appeared to be a novel NADPH-UQ oxidoreductase and responsible for the UQ redox state in liver.
引用
收藏
页码:331 / 334
页数:4
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