Inhibition of Halobacterium cutirubrum Lipid Biosynthesis by Bacitracin
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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 کاملHALOBACTERIUM CUTIRUBRUM DEOXYRIBONUCLEIC ACID-DEPENDENT RIBONUCLEIC ACID POLYMERASE By B. GREGORY LOUIS AND P. S. FITT
1. DNA-dependent RNA polymerase was purified 150-fold from crude extracts of the extreme halophile Halobacterium cutirubrum. 2. The enzyme requires the presence of native DNA and all four nucleoside triphosphates to incorporate '4C-labelled nucleoside triphosphate into an acid-insoluble ribonuclease-sensitive product. 3. It has an absolute requirement for both Mn2+ and Mg2+. 4. The polymerase r...
متن کاملInhibition of Cuticular Lipid Biosynthesis in Pisum sativum by Thiocarbamates.
Treatment of slices of young pea leaves (Pisum sativum) with muM solutions of alpha-chlorallyl diethyldithiocarbamate, dichloroallyl diisopropylthiocarbamate, or S-ethyldipropylthiocarbamate resulted in inhibition of incorporation of [1-(14)C]acetate into C(31) alkane and C(31) secondary alcohol, very little effect on the synthesis of C(26) and C(28) fatty alcohols, and an accumulation of (14)C...
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.
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ژورنال
عنوان ژورنال: Journal of General Microbiology
سال: 1979
ISSN: 0022-1287
DOI: 10.1099/00221287-111-2-423