Thymidine kinase from Tetrahymena thermophila. Purification and immunological analysis
نویسندگان
چکیده
منابع مشابه
Tetrahymena thermophila
What does it look like? Tetrahymena thermophila is a unicellular eukaryote which is larger than many mammalian cells (~30 × 50 μm). It swims in temperate freshwater environments, waving its coat of cilia (Figure 1, inset) and phagocytosing food propelled into its gullet. Hunger induces Tetrahymena cells to undergo a transformation, including growth of a long posterior cilium and more coordinate...
متن کاملComprehensive phosphoprotein analysis of linker histone H1 from Tetrahymena thermophila.
Linker histone H1 is highly phosphorylated in normal growing Tetrahymena thermophila but becomes noticeably dephosphorylated in response to certain conditions such as prolonged starvation. Because phosphorylation of H1 has been associated with the regulation of gene expression, DNA repair, and other critical processes, we sought to use mass spectrometry-based approaches to obtain an in depth ph...
متن کاملAdolescence in Tetrahymena thermophila.
The development of sexual maturity in Tetrahymena thermophila has been shown to include an intermediate stage, adolescence, during which cells are capable of mating with mature cells but not other adolescent cells. When the progeny of successfully mated cells are grown logarithmically and tested frequently for the ability to mate, they are unable to form mating pairs for about 65 generations. T...
متن کاملPurification, characterization and molecular cloning of TGP1, a novel G-DNA binding protein from Tetrahymena thermophila.
G-DNA, a polymorphic family of four-stranded DNA structures, has been proposed to play roles in a variety of biological processes including telomere function, meiotic recombination and gene regulation. Here we report the purification and cloning of TGP1, a G-DNA specific binding protein from Tetrahymena thermophila. TGP1 was purified by three-column chromatographies, including a G-DNA affinity ...
متن کاملPurification and partial characterization of glyceraldehyde-3-phosphate dehydrogenase from the ciliate Tetrahymena thermophila.
In the present study, we purified the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) which is involved in cellular energy production and has important housekeeping functions, from the ciliate Tetrahymena thermophila using a three-step procedure. The enzyme was purified ~68 folds by ammonium sulfate precipitation, followed by two steps of column chromatography (DEAE-cellulose...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1991
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1991.tb15675.x