ENZYMIC SYNTHESIS OF DIMETHYL SELENIDE FROM SODIUM SELENITE IN MOUSE LIVER EXTRACTS
ENZYMIC SYNTHESIS OF DIMETHYL SELENIDE FROM SODIUM SELENITE IN MOUSE LIVER EXTRACTS
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DOI:
10.1021/bi00867a039
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发表时间:
1966-01-01
期刊:
影响因子:
2.9
通讯作者:
GANTHER, HE
中科院分区:
文献类型:
--
作者:
GANTHER, HE
The enzymic synthesis of dimethyl selenide from sodium selenite was studied with mouse liver extracts as a model system for the reductive utilization of selenium. Dimethyl selenide was identified as the major volatile product in doubly labeled studies with carbon-14 and selenium-75. Both the 165,000 x g supernatant fraction of liver and washed microsomes synthesize dimethyl selenide, but neither fraction is as active as a 9000 x g supernatant fraction. Activity is proportional to protein concentration, and heated extracts are inactive. Optimal conditions were determined for the over-all reaction. The crude system has a specific requirement for glutathione that cannot be eliminated by various thiols or by dithiothreitol. S-Adenosyl-L-methionine is the probable methyl donor. Reduced triphosphopyridine nucleotide, co-enzyme A, adenosine 5[image]-triphosphate, and Mg are also required for optimal activity. Incubation under N increases the yield of dimethyl selenide approximately 10-fold compared to incubation in air, apparently by preventing the oxidation of labile reduced forms of S. The crude system is inhibited 50% by 10-6 M arsenite in the presence of a large excess of thiols and is also inhibited by Cd. The possible role of glutathione derivatives of Se in the synthesis of organoselenium compounds is discussed.