| Literature DB >> 12382120 |
Moeava Tehei1, Bruno Franzetti, Marie-Christine Maurel, Jacques Vergne, Codjo Hountondji, Giuseppe Zaccai.
Abstract
Trapping malate dehydrogenase from the extremely halophilic archaeon Haloarcula marismortui in "dry" salt crystals protects the enzyme against thermal denaturation. Similar protection was not observed for the homologous mesophilic enzyme. In the case of transfer RNA molecules, high salt concentration plays a protective role against thermal degradation allowing activity to be recovered. The results are discussed in the context of exploring the fate of cell-free biological macromolecules in the environment and that of orienting the search for traces of life in planetary exploration.Entities:
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Year: 2002 PMID: 12382120 DOI: 10.1007/s00792-002-0275-6
Source DB: PubMed Journal: Extremophiles ISSN: 1431-0651 Impact factor: 2.395