Literature DB >> 3054074

Plasmodium falciparum: association with erythrocytic superoxide dismutase.

A E Arias1, R D Walter.   

Abstract

Levels of superoxide dismutase (SOD) activity and its properties in Plasmodium falciparum-infected erythrocytes, isolated parasites, and noninfected erythrocytes were studied. A higher specific activity was found in P. falciparum-infected erythrocytes compared to noninfected erythrocytes, resulting from the lower protein content of infected cells and not enzyme synthesis by the parasite, as the superoxide dismutase activity expressed per number of cells was decreased. Superoxide dismutase from noninfected erythrocytes and isolated P. falciparum parasites showed similar sensitivities to various inhibitors and had identical molecular weights and electrophoretic mobilities. These results support the hypothesis of uptake and use of the erythrocytic SOD enzyme by the parasite as a possible mechanism of defense against oxidative stress.

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Year:  1988        PMID: 3054074     DOI: 10.1111/j.1550-7408.1988.tb04104.x

Source DB:  PubMed          Journal:  J Protozool        ISSN: 0022-3921


  2 in total

1.  Characterization and molecular cloning of a Cu/Zn superoxide dismutase from the human parasite Onchocerca volvulus.

Authors:  K J Henkle; E Liebau; S Müller; B Bergmann; R D Walter
Journal:  Infect Immun       Date:  1991-06       Impact factor: 3.441

2.  Quantitative time-course profiling of parasite and host cell proteins in the human malaria parasite Plasmodium falciparum.

Authors:  Bernardo Javier Foth; Neng Zhang; Balbir Kaur Chaal; Siu Kwan Sze; Peter Rainer Preiser; Zbynek Bozdech
Journal:  Mol Cell Proteomics       Date:  2011-05-10       Impact factor: 5.911

  2 in total

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