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. 1979 Feb 1;177(2):441–448. doi: 10.1042/bj1770441

Simple efficient methods for the isolation of malate dehydrogenase from thermophilic and mesophilic bacteria.

I P Wright, T K Sundaram
PMCID: PMC1186393  PMID: 435244

Abstract

Malate dehydrogenase from a number of bacteria drawn from several genera and representing the mesophilic, moderately thermophilic and extremely thermophilic classes was isolated by procedures which involve only a small number of steps (in most cases only two), of which the key one is affinity chromatography on 5'-AMP--Sepharose and/or on NAD+--hexane--agarose. Electrophoretic analysis of the native enzymes in polyacrylamide gel and of the denaturated enzymes in sodium dodecyl sulphate/polyacrylamide gel revealed no significant protein impurity in the purified preparations. The yields ranged from about 40% to over 80%. The malate dehydrogenases from the extreme thermophiles and from some of the moderate thermophiles are appreciably less efficient catalytically than their mesophilic homologues.

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Selected References

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