The 5-S RNA . Protein Complex from an Extreme Halophile, Halobacterium cutirubrum. Purification and Characterization
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چکیده
منابع مشابه
The 5 S RNA.protein complex from an extreme halophile, Halobacterium cutirubrum. Studies on the RNA-protein interaction.
A 5-S RNA . protein complex has been isolated from the 50-S ribosomal subunit of an extreme halophile, Halobacterium cutirubrum. The 50-S ribosomal subunit from the extreme halophile requires 3.4 M K+ and 100 mM Mg2+ for stability. However, if the high K+ concentration is maintained but the Mg2+ concentration lowered to 0.3 mM, the 5-S RNA . protein complex is selectively extracted from the sub...
متن کاملEffect of monovalent cations on the malic enzyme from the extreme halophile, Halobacterium cutirubrum.
The malic enzyme from Halobacterium cutirubrum requires monovalent cations for both activation and stabilization. NaCl, the best stabilizer, is ineffective as activator; NH(4)Cl, the best activator, is a poor stabilizer. These results support the idea that the roles of salts in both processes are different.
متن کاملStructure determination of the glycolipid sulfate from the extreme halophile Halobacterium cutirubrum.
A sulfur-containing glycolipid, accounting for ca. 25% of the total polar lipids, has been isolated from the extreme halophile Halobacterium cutirubrum. The ammonium salt of the lipid was found to have the molecular formula C(61)H(117)O(21)S.NH(4), and on strong acid hydrolysis it yielded 2,3-di-O-phytanyl-sn-glycerol, glucose, mannose, galactose, and sulfate in equimolar proportions. Infrared ...
متن کاملMechanism of dissolution of envelopes of the extreme halophile Halobacterium cutirubrum.
Onishi, H. (National Research Council, Ottawa, Ontario, Canada), and D. J. Kushner. Mechanism of dissolution of envelopes of the extreme halophile Halobacterium cutirubrum. J. Bacteriol. 91:646-652. 1966.-Envelopes of Halobacterium cutirubrum dissolved rapidly in media of low ionic strength. Heating partially inhibited breakdown, probably because of nonspecific protein coagulation rather than i...
متن کاملPartial purification and properties of Halobacterium cutirubrum L-alanine dehydrogenase.
1. Halobacterium cutirubrum L-alanine dehydrogenase was purified approx. 100-fold. 2. It has a mol. wt. of 72 500, about one-third that of two well-studied alanine dehydrogenases from non-halophiles. 3. The activity of the enzyme increases with temperature up to 70 degrees C, but the protein itself is not thermostable. 4. In the reductive amination reaction, the enzyme is fully active in the pr...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1978
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1978.tb12554.x