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- W93915713 abstract "The cytochrome oxidase (EC 1.9.3.1) of Thermusthermophilus HB8 was isolated from the membrane fraction, and was highly purified. The oxidase contained heme a and heme c as the prosthetic groups. The purified preparation showed a single band in polyacrylamide gel electrophoresis, and three major polypeptides with apparent molecular weights of 52,000, 37,000 and 29,000 were observed in the presence of sodium dodecyl sulfate. The enzyme reacted rapidly with T. thermophilus cytochrome c-552. The oxidation of T. thermophilus cytochrome c-555,549 by the enzyme was very slow, and was stimulated by the addition of cytochrome c-552. The enzyme was highly stable to heat." @default.
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- W93915713 date "1980-02-01" @default.
- W93915713 modified "2023-09-25" @default.
- W93915713 title "Cytochrome oxidase from an extreme thermophile, Thermusthermophilus HB 8" @default.
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- W93915713 doi "https://doi.org/10.1016/0006-291x(80)90804-9" @default.
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