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Journal of Molecular Evolution

, Volume 19, Issue 5, pp 371–375 | Cite as

Glutathione reductase in evolution

  • R. N. Ondarza
  • J. L. Rendón
  • M. Ondarza
Original Articles

Summary

The disulfide reducing activities of GSSG-and CoASSG-reductases were measured on partially purified extracts from a variety of prokaryotes and eukaryotes.

Glutathione-reductase was found in varying amounts in all eukaryotes and prokaryotes, used in this study, with the exception of the two strict anaerobesClostridium tartarivorum andDesulfovibrio vulgaris, and the two primitive ArchaebacteriaMethanosarcina barkeri andHalobacterium halobium.

CoASSG-reductase was found in some eukaryotes and prokaryotes, but showed no clear pattern of distribution other than its absence whenever GSSG-reductase was not present.

The absence of GSSG-reductase activity in organisms lacking GSH, confirms that glutathione metabolism is not universal and suggests that this enzyme might be useful as a marker in classifying organisms. The data suggest that glutathione-reductase occurs as a result of the change from a reducing to a oxidizing atmosphere in the primitive Earth.

Key words

Disulfide reductase Glutathione Atmospheric oxygen Microbial evolution Prokaryoteseukaryotes 

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Copyright information

© Springer-Verlag 1983

Authors and Affiliations

  • R. N. Ondarza
    • 1
  • J. L. Rendón
    • 2
  • M. Ondarza
    • 1
  1. 1.Scripps Institution of OceanographyUniversity of California at La JollaUSA
  2. 2.Faculty of Medicine, Department of Biochemistry and Experimental BiologyNational Autonomous University of MexicoMexico City

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