Thermostable Aldolase from Thermus aquaticus
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چکیده
منابع مشابه
Thermostable aldolase from Thermus aquaticus.
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...
متن کاملPurification by affinity chromatography of thermostable glyceraldehyde 3-phosphate dehydrogenase from Thermus aquaticus.
activities of the key enzymes of gluconeogenesis in the liver and kidney of the foetal guinea pig have been followed. The foetal guinea pigs used had a gestational age of 68-72 days. Pyruvate carboxylase was present at very low activities in the kidney of the foetus and neonatal animal and also in the foetal liver until day 50, when it increased in activity to reach a value by day 60 of more th...
متن کاملOligomerization of a MutS mismatch repair protein from Thermus aquaticus.
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...
متن کاملCharacterization of functionally active subribosomal particles from Thermus aquaticus.
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 ...
متن کاملConformational 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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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1970
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.101.2.541-550.1970