Results 261 to 270 of about 40,909 (278)
Some of the next articles are maybe not open access.
A DNA Methylase from Thermus thermophilus HB8
The Journal of Biochemistry, 1980A DNA methylase was purified in a homogeneous state from a extremely thermophilic bacterium, Thermus thermophilus HB8, by chromatography on, successively, phosphocellulose, CM-cellulose, and heparin-Sepharose. The molecular weight of the enzyme was determined to be about 44,000 by gel filtration on a Sephadex G-100 column and 41,000 by SDS-poly ...
Kayoko Nakazawa+2 more
openaire +3 more sources
Journal of Biochemistry (Tokyo), 2015
Dihydrouridine (D) is formed by tRNA dihydrouridine synthases (Dus). In mesophiles, multiple Dus enzymes bring about D modifications at several positions in tRNA.
Hiroaki Kusuba+8 more
semanticscholar +1 more source
Dihydrouridine (D) is formed by tRNA dihydrouridine synthases (Dus). In mesophiles, multiple Dus enzymes bring about D modifications at several positions in tRNA.
Hiroaki Kusuba+8 more
semanticscholar +1 more source
Inhibitors of Thermus thermophilus Isopropylmalate Dehydrogenase
The Journal of Organic Chemistry, 1994In an attempt to use mechanism-based design for the discovery of inhibitors of the isopropylmalate dehydrogenase from T. thermophilus, we have prepared and studied a number of potential mimics for an intermediate in the oxidative decarboxylation of isopropyl malate, the enol or enolate of α-ketoisocaproate. Because hydroramate and dicarboxylate enolate
Michael C. Pirrung+2 more
openaire +2 more sources
Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus
Nature Structural Biology, 1995The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus, solved at 2.9 A resolution, displays (alpha beta)2 subunit organization. Unexpectedly, both the catalytic alpha- and the non-catalytic beta-subunits comprise the characteristic fold of the class II active-site domains.
Mosyak, Lidia+4 more
openaire +4 more sources
A hyperthermophilic laccase from Thermus thermophilus HB27
Extremophiles, 2005A copper-inducible laccase activity was detected in Thermus thermophilus HB27. The enzyme was partially purified and separated by SDS-PAGE. After staining, a gel slice containing a approximately 53-kDa protein was excised and treated with trypsin, and the in-gel digests were analyzed by mass spectrometry. By mass fingerprinting, the peptides were found
openaire +3 more sources
Biochemical Assays of Gre Factors of Thermus Thermophilus
2003Publisher Summary This chapter discusses the biochemical assaying of Gre factors of Thermus Thermophilus. The biochemical studies of Escherichia coli Gre factors indicate that they are not nucleases but RNAP co-factors, which activate the same catalytic center involved in both RNA synthesis and RNA hydrolysis reactions.
Sergei Borukhov, Oleg Laptenko
openaire +3 more sources
Biotechnological Applications of Thermus thermophilus as Host
Current Biotechnology, 2013Aurelio Hidalgo, Jose Berenguer
openaire +2 more sources
Genes and Genetic Manipulation in Thermus thermophilus
1995Nagahari and colleagues (1980) first isolated a gene from Thermus by cloning a HindIII fragment of chromosomal DNA containing the leuCine genes, leuB, leuC, and leuD from Thermus thermophilus strain HB27 into Escherichia coli. Independently, Tanaka et al.
openaire +2 more sources
Purification of Hsp60 from Thermus thermophilus
2003Andrzej Joachimiak, Elsie Quaite-Randall
openaire +2 more sources