In:
FEBS Letters, Wiley, Vol. 314, No. 3 ( 1992-12-21), p. 331-334
Abstract:
Ubiquinone (UQ) reductase activity which reduces UQ to ubiquinol (UQH 2 ) in rat tissues was roughly proportional to the UQH 2 /total UQ ratio in respective tissues. The honest activity was found in the liver, showing the highest UQH 2 /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°C. The DT‐diaphorase activity was stable. UQ reductase required NADPH as the hydrogen donor and was not inhibited by a less than 1μM 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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(92)81499-C
Language:
English
Publisher:
Wiley
Publication Date:
1992
detail.hit.zdb_id:
212746-5
detail.hit.zdb_id:
1460391-3
SSG:
12
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