Transfer of transposon Tn916 from Bacillus subtilis to Thermus aquaticus
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چکیده
منابع مشابه
Conformational stability of lactate dehydrogenase from Bacillus thermus-aquaticus [proceedings].
Proteins are synthesized and enzymes can function at surprisingly high temperatures in thermophilic micro-organisms. This temperature is about 90°C in the case of Bacillus thermus-aquaticus (A.T.C.C. 25104). Lactate dehydrogenase (EC 1.1.1.27) was isolated from this micro-organism, and the temperature dependence of the rate of pyruvate reduction and thermodynamic parameters of heat inactivation...
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Data are presented on the purification and properties of the thermostable fructose-1,6-diphosphate aldolase of Thermus aquaticus, a nonsporulating, extreme thermophile. The enzyme shows little activity at temperatures below 60 C and optimal activity at about 95 C. The enzyme was purified 43-fold by diethylaminoethyl cellulose column chromatography and Sephadex G-200 gel filtration. The enzyme i...
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The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases. We have examined the oligomerization of a MutS protein from Thermus aquaticus that binds to heteroduplex DNAs at elevated temperatures. Analytical gel filtration, cross-linking of MutS protein with disuccinimidyl suberate, light scattering, and matrix-assisted laser desorption/ionization time-of-f...
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Peptidyl transferase activity of Thermus aquaticus ribosomes is resistant to the removal of a significant number of ribosomal proteins by protease digestion, SDS, and phenol extraction. To define the upper limit for the number of macromolecular components required for peptidyl transferase, particles obtained by extraction of T. aquaticus large ribosomal subunits were isolated and their RNA and ...
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ژورنال
عنوان ژورنال: FEMS Microbiology Letters
سال: 1990
ISSN: 0378-1097
DOI: 10.1111/j.1574-6968.1990.tb13849.x