نتایج جستجو برای: thermus aquaticus

تعداد نتایج: 2175  

2010
Ramon Kranaster

" One-step RNA pathogen detection with reverse transcriptase activity of a mutated thermostable Thermus aquaticus DNA polymerase. " EMBO through an abasic DNA lesion: structural basis for adenine selectivity. " A. " Mutant DNA polymerase for improved detection of single-nucleotide variations in microarrayed primer extension " Chem. Eur. A. " Increased single-nucleotide discrimination in allele-...

Journal: :Bioscience, biotechnology, and biochemistry 1998
T Tanaka H Matsuzawa T Ohta

Aqualysin I is the alkaline serine protease isolated from an extreme thermophile, Thermus aquaticus YT-1. We analyzed kinetic properties of aqualysin I, using sixteen kinds of chromogenic succinyl-tripeptide p-nitroanilides as substrates. And we compared the substrate specificity of aqualysin I with those of proteinase K, subtilisin BPN', and subtilisin Carlsberg. We found that aqualysin I had ...

Journal: :Cell 2001
Elizabeth A. Campbell Nataliya Korzheva Arkady Mustaev Katsuhiko Murakami Satish Nair Alex Goldfarb Seth A. Darst

Rifampicin (Rif) is one of the most potent and broad spectrum antibiotics against bacterial pathogens and is a key component of anti-tuberculosis therapy, stemming from its inhibition of the bacterial RNA polymerase (RNAP). We determined the crystal structure of Thermus aquaticus core RNAP complexed with Rif. The inhibitor binds in a pocket of the RNAP beta subunit deep within the DNA/RNA chann...

Journal: :Biochemical Society transactions 1978
S Lakatos G Halász P Závodszky

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...

Journal: :Science 1988
R K Saiki D H Gelfand S Stoffel S J Scharf R Higuchi G T Horn K B Mullis H A Erlich

A thermostable DNA polymerase was used in an in vitro DNA amplification procedure, the polymerase chain reaction. The enzyme, isolated from Thermus aquaticus, greatly simplifies the procedure and, by enabling the amplification reaction to be performed at higher temperatures, significantly improves the specificity, yield, sensitivity, and length of products that can be amplified. Single-copy gen...

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