Halophilic malate dehydrogenase--a case history of biophysical investigations: ultracentrifugation, light-, X-ray- and neutron scattering.
Biochem Soc Symp
; 58: 113-25, 1992.
Article
em En
| MEDLINE
| ID: mdl-1445401
ABSTRACT
Halophilic malate dehydrogenase (hMDH) from Haloarcula marismortui has been isolated, purified and characterized by biochemical and biophysical solution studies. A stabilization mechanism at extremely high concentrations of salt, based on the formation of co-operative hydrate bonds between the protein and hydrated salt ions, was suggested from thermodynamic analysis of native enzyme solutions. Recently the gene coding for hMDH was isolated and sequenced and an active enzyme cloned (F. Cendrin, J. Chroboczek, G. Zaccai, H. Eisenberg and M. Mevarech, unpublished work). A study of the crystal structure of hMDH in a high-salt physiological medium is in progress (O. Butbul-Dym & J. Sussman, personal communication). Here we discuss in depth implications of these recent developments on our earlier results.
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Base de dados:
MEDLINE
Assunto principal:
Halobacteriaceae
/
Malato Desidrogenase
Idioma:
En
Revista:
Biochem Soc Symp
Ano de publicação:
1992
Tipo de documento:
Article
País de afiliação:
Israel