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Solution studies malate dehydrogenase

Malate dehydrogenase from H. marismortui (AMDH) is the halophilic protein that has been studied most by solution structure methods. A molar mass of 87 kg/mol was determined for the native enzyme. It is stable at high concentrations of NaCl or KC1 and unfolds and dissociates below 2.5 M salt. Pundak and Eisenberg (1981) first measured values for the solvent interactions of AMDH and found that, in contrast to nonhalophilic globular proteins in similar conditions (Bi 0.2—0.3 g/g,B3 0.01 g/g),the halophilic protein bound... [Pg.36]

See other pages where Solution studies malate dehydrogenase is mentioned: [Pg.2]    [Pg.42]    [Pg.324]    [Pg.325]    [Pg.107]    [Pg.445]    [Pg.617]    [Pg.28]    [Pg.30]    [Pg.371]    [Pg.116]    [Pg.201]   


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Dehydrogenases studies

Malate

Malate dehydrogenase

Malates

Solution studies

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