Ecophysiology of Bacteriophage S5100 Infecting Halobacterium cutirubrum
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چکیده
منابع مشابه
Partial 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...
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 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 کاملPurification and properties of the ribonucleic acid-dependent ribonucleic acid polymerase from Halobacterium cutirubrum.
1. The RNA-dependent RNA polymerase from Halobacterium cutirubrum was purified to electrophoretic homogeneity. 2. It requires a single-stranded molecule of RNA or polyribonucleotide as template. 3. Nearest-neighbour analyses of the products formed on random poly(A,U) or alternating poly(A-U) templates and base analysis of the product of synthesis directed by wheat-germ RNA prove that the templa...
متن کاملEffect of salts and organic solvents on the activity of Halobacterium cutirubrum catalase.
Catalase in extracts of the extreme halophile Halobacterium cutirubrum exhibits up to threefold stimulation by 0.5 to 1.5 m monovalent salts and by 0.1 m divalent salts. Above these concentrations, inhibition of enzyme activity is observed. The inhibitory effect, and to some extent the stimulation, is salt-specific; the effectiveness of a salt in inhibiting enzyme activity depends on both catio...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1990
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.56.11.3605-3608.1990