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- W2034673370 abstract "Abstract 1. 1.|Enzymatic activities responsible for H 2 S production in various tissues were compared. The distribution of 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2) correlated with the estimated labile sulfur contents in each tissue, however, that of thiosulfate sulfurtransferase (EC 2.8.1.1) did not correlate at all, being extremely high in liver and kidney. Therefore, it is unlikely that thiosulfate sulfurtransferase is responsible for iron sulfur chromophore formation. 2. 2.|The subcellular distribution of 3-mercaptopyruvate sulfurtransferase and transaminase activities shows that cysteine transamination occurs in cytosol and then 3-mercaptopyruvate so formed would be degraded to pyruvate and H 2 S by cytosol 3-mercaptopyruvate sulfurtransferase. However, the possibility that mitochondrial 3-mercaptopyruvate sulfurtransferase is involved in the degradation of 3-meraptopyruvate within mitochondria cannot be excluded. 3. 3.|Upon incubation of the apoprotein with 3-mercaptopyruvate and purified 3-mercaptopyruvate sulfurtransferase or cystein, α-ketoglutarate, transaminase and 3-mercaptopyruvate sulfurtransferase in the presence of iron and thiol- compounds, the reconstitution of iron-sulfur chromophore could be achieved. 4. 4.|From these results, it is concluded that 3-mercaptopyruvate sulfurtransferase plays a role in iron-sulfur chromophore formation in adrenal cortex." @default.
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- W2034673370 title "Role of 3-mercaptopyruvate sulfurtransferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin" @default.
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- W2034673370 doi "https://doi.org/10.1016/0005-2744(74)90014-x" @default.
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