Halobacterium cutirubrum tRNA sequences

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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...

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Mechanism of dissolution of envelopes of the extreme halophile Halobacterium cutirubrum.

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Effect of monovalent cations on the malic enzyme from the extreme halophile, Halobacterium cutirubrum.

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Purification 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...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1985

ISSN: 0014-5793

DOI: 10.1016/0014-5793(85)80164-2