| Literature DB >> 14329441 |
Abstract
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.Entities:
Keywords: ACETONE; CHEMISTRY; CHEMISTRY, ANALYTICAL; CHROMATOGRAPHY; DIALYSIS; ELECTROPHORESIS; EXPERIMENTAL LAB STUDY; HALOBACTERIUM; HYDROGEN-ION CONCENTRATION; MALATE DEHYDROGENASE; METABOLISM; NAD; SODIUM CHLORIDE
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Year: 1965 PMID: 14329441 PMCID: PMC315644 DOI: 10.1128/jb.90.2.312-315.1965
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490