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- W2021844965 abstract "A metalloprotein with superoxide dismutase activity was isolated and purified from muscle-stage Trichinella spiralis. The anti-genicity of the purified enzyme was demonstrated by an immunospecific reaction with T. spiralis antiserum in an enzyme-linked immunosorbent assay. In addition to its presence in somatic extracts of T. spiralis, the enzyme was also excreted into culture fluids in which the muscle-stage larvae had been incubated for periods as short as 3 hr and up to 72 hr. The enzyme was characterized as a copper- and zinc-containing, cyanide-sensitive, superoxide dismutase with a molecular weight of 36,000 (estimated by get filtration), consisting of two subunits of 17,000 Mr (estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis). The isoelectric point was 5.6. Muscle-stage T. spiralis contained one molecular form of the enzyme, whereas adult T. spiralis contained two molecular forms. This enzyme may function as an essential defense mechanism against the highly destructive superoxide radical encountered either intracellularly, as a product of biological oxidation, or externally, as a component of the host's immune system." @default.
- W2021844965 created "2016-06-24" @default.
- W2021844965 creator A5081155836 @default.
- W2021844965 date "1983-08-01" @default.
- W2021844965 modified "2023-09-27" @default.
- W2021844965 title "Trichinella spiralis: Identification and purification of superoxide dismutase" @default.
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- W2021844965 doi "https://doi.org/10.1016/0014-4894(83)90095-4" @default.
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