Properties of a Purified Halophilic Malic Dehydrogenase
Properties of a Purified Halophilic Malic Dehydrogenase
复制标题
纯化的嗜盐苹果酸脱氢酶的特性
DOI:
10.1128/jb.90.2.316-326.1965
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发表时间:
1965
影响因子:
3.2
通讯作者:
H. Halvorson
中科院分区:
文献类型:
--
作者:
P. K. Holmes;H. Halvorson
Holmes, P. K. (University of Illinois, Urbana), and H. Orin Halvorson. Properties of a purified halophilic malic dehydrogenase. J. Bacteriol. 90:316–326. 1965.—The malic dehydrogenase (MDH) from Halobacterium salinarium required high concentrations of monovalent ions for stability and activity. Studies of inactivation rates at different salt concentrations suggested that approximately 25% NaCl (w/v) is required to stabilize MDH. From 50 to 100% reactivation, depending on the salt concentration present during inactivation, could occur in 2.5 to 5 m NaCl or KCl. The optimal salt concentration for activity of MDH was a function of the pH, and ranged from 1 to 3 m NaCl or KCl. The effect of salt concentration on the pH-activity curves occurred chiefly below pH 7.0. Inactivation of MDH with heat or thiol reagents showed that the enzyme was more labile in the state induced by absence of salt. The activation of MDH by salts was attributed to a decreased rate of dissociation of MDH and reduced nicotinamide adenine dinucleotide (NADH2). The inactivation of the enzyme in the absence of salt could be largely prevented by the presence of NADH2. The S20.w of MDH decreased threefold at low salt concentrations. The enzyme was assumed to be in its native compact configuration only in the presence of a high concentration of salt.