PURIFICATION OF A SALT-REQUIRING ENZYME FROM AN OBLIGATELY HALOPHILIC BACTERIUM.
Holmes, P. K. (University of Illinois, Urbana), and H. O. Halvorson. Purification of a salt-requiring enzyme from an obligately halophilic bacterium. J. Bacteriol. 90: 312-315. 1965.-The discovery that some halophilic enzymes may be reactivated from the salt-free and inactive state has facilitated the purification of nicotinamide adenine dinucleotide-linked malic acid dehydrogenase from crude extracts of Halobacterium salinarium. In the absence of large amounts of salt, the enzyme was totally inactive; yet, in this salt-free state, it could be purified by conventional techniques. The highly purified halophilic enzyme was shown to require a high concentration of salt for activity.
D000096:Acetone; D001419:Bacteria; D055598:Chemical Phenomena; D002621:Chemistry; D002623:Chemistry Techniques, Analytical; D002845:Chromatography; D003956:Dialysis; D004586:Electrophoresis; D006217:Halobacterium; D019617:Halobacterium salinarum; D006863:Hydrogen-Ion Concentration; D008291:Malate Dehydrogenase; D008660:Metabolism; D009243:NAD; D006435:Renal Dialysis; D012106:Research; D012965:Sodium Chloride
D009243:NAD; D000096:Acetone; D012965:Sodium Chloride; D008291:Malate Dehydrogenase
ACETONE; CHEMISTRY; CHEMISTRY, ANALYTICAL; CHROMATOGRAPHY; DIALYSIS; ELECTROPHORESIS; EXPERIMENTAL LAB STUDY; HALOBACTERIUM; HYDROGEN-ION CONCENTRATION; MALATE DEHYDROGENASE; METABOLISM; NAD; SODIUM CHLORIDE